Plants with Increased Yield

ABSTRACT

This invention relates generally to a plant cell with enhanced nitrogen use efficiency and/or increased biomass production as compared to a corresponding non-transformed wild type plant cell by increasing or generating one or more activities of polypeptides associated with enhanced nitrogen use efficiency in plants.

RELATED APPLICATIONS

This application is a divisional application of U.S. patent applicationSer. No. 12/678,387, filed on Mar. 16, 2010, which is a national stageapplication (under 35 U.S.C. §371) of PCT/EP2008/062362, filed Sep. 17,2008, which claims benefit of European application 07117448.6, filedSep. 18, 2007 and European application 08161134.5, filed Jul. 25, 2008.The entire contents of each of these applications are herebyincorporated by reference herein in their entirety.

SUBMISSION OF SEQUENCE LISTING

The Sequence Listing associated with this application is filed inelectronic format via EFS-Web and hereby incorporated by reference intothe specification in its entirety. The name of the text file containingthe Sequence Listing is Sequence_Listing_(—)13987_(—)00234. The size ofthe text file is 68,247 KB, and the text file was created on Jan. 8,2014.

The present invention pertains to the field of molecular biology, plantgenetics, plant physiology and developmental biology. More specifically,the present invention disclosed herein provides plant cells comprisingnucleic acids enhancing or improving one or more traits of a transgenicplant, plants comprising such cells, progeny, seed and pollen derivedfrom such plants, and methods of making and methods of using such plantcell(s) or plant(s), progeny, seed(s) or pollen. Particularly, saidimproved trait(s) are manifested in an increased yield, preferably byimproving one or more yield-related trait(s).

Under field conditions, plant performance, for example in terms ofgrowth, development, biomass accumulation and seed generation, dependson a plant's tolerance and acclimation ability to numerous environmentalconditions, changes and stresses. Since the beginning of agriculture andhorticulture, there was a need for improving plant traits in cropcultivation. Besides increasing yield by applying technical advances incrop planting, breeding strategies foster crop properties to withstandbiotic and abiotic stresses, to increase nutrient use efficiency and toalter other crop specific yield parameters. The intrinsic growth anddevelopment characteristics of plants are improved, tolerance to bioticand abiotic stresses are introduced to maintain yield underenvironmental stress conditions and to extend acreage under differentclimatic situations. Crops with better nutrient use efficiency aredeveloped to reduce fertilizer input and also to extend acreage intoregions with nutrient poor soil.

Plants are sessile organisms and consequently need to cope with variousenvironmental stresses. Biotic stresses such as plant pests andpathogens on the one hand, and abiotic environmental stresses on theother hand are major limiting factors of plant growth and productivity(Boyer, Plant Productivity and Environment, Science 218, 443-448 (1982);Bohnert et al., Adaptations to Environmental Stresses, Plant Cell 7 (7),1099-1111 (1995)), thereby limiting plant cultivation and geographicaldistribution. Plants exposed to the different stresses typically havelow yields of plant material, seeds, fruit and other products. Croplosses and crop yield losses of e.g. major crops such as rice, maize(corn), oil seed rape (including winter oil seed rape and canola),cotton, soybean and wheat caused by these stresses represent asignificant economic and political factor and contribute to foodshortages, particularly in many underdeveloped countries.

Conventional means for crop and horticultural improvements today utilizeselective breeding techniques to identify plants with desirablecharacteristics. Such conventional techniques, however, have severaldrawbacks. Very often plants contain heterogeneous genetic componentsthat may not always result in the desirable trait being passed on fromparent plants, particularly not without other negative impacts. Thus,particularly complex traits such as yield and stress phenomena makegenetic optimization by traditional breeding approaches difficult,costly and time-consuming. On the contrary, advances in molecularbiology have allowed modifying the germplam of plants in a specific way.The modification of a single gene, for example, resulted in severalcases in a significant increase in e.g. stress tolerance (Wang et al.,2003) and other yield-related traits. As different plants have to resistdifferent kinds and strengths of stress in different cultivation areasthere is still a need to identify genes which show various combinationsof stress resistance to produce optimal yield. There is still a need toidentify genes which have the overall capacity to improve yield ofplants.

The present invention provides transgenic plant nuclei and/or transgenicplant cells comprising one or more nucleic acid(s) which enhances orimproves one or more trait(s) of a transgenic plant, plants comprisingsuch cells, progeny, seed and pollen derived from such plants, andmethods of making and methods of using such plant cell(s) or plant(s),progeny, seed(s) or pollen. Particularly, said improved trait(s) aremanifested in an increased yield.

In one embodiment, the present invention provides a method for producingsuch transgenic plant cell(s) or plant(s) with increased yield byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

In a further embodiment, the activity is increased by increasing theamount and/or activity of one or more protein(s) having an activityselected from the group consisting of 2-dehydro-3-deoxy-phosphoheptonatealdolase, 3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease; and wherein such one or moreprotein(s) each comprises a polypeptide as depicted in table II, column5 or 7.

Said increased yield in accordance with the present invention cantypically be achieved by enhancing or improving, in comparison to anon-transformed starting or wild-type plant, one or more yield-relatedtraits of a plant. Such yield-related traits of a plant the improvementof which results in increased yield comprise, without limitation, theincrease of the intrinsic yield capacity of a plant, improved nutrientuse efficiency, and/or increased stress tolerance.

According to the present invention, yield-related traits concerning anincrease of the intrinsic yield capacity of a plant may be manifested byimproving the specific (intrinsic) seed yield (e.g. in terms ofincreased seed/grain size, increased ear number, increased seed numberper ear, improvement of seed filling, improvement of seed composition,embryo and/or endosperm improvements, or the like); modification andimprovement of inherent growth and development mechanisms of a plant(such as plant height, plant growth rate, pod number, pod position onthe plant, number of internodes, incidence of pod shatter, efficiency ofnodulation and nitrogen fixation, efficiency of carbon assimilation,improvement of seedling vigour/early vigour, enhanced efficiency ofgermination (under stressed or non-stressed conditions), improvement inplant architecture, cell cycle modifications, photosynthesismodifications, various signaling pathway modifications, modification oftranscriptional regulation, modification of translational regulation,modification of enzyme activities, and the like); and/or the like.

According to the present invention, yield-related traits concerning animprovement or increase in nutrient use efficiency of a plant may bemanifested by improving a plant's general efficiency of nutrientassimilation (e.g. in terms of improvement of general nutrient uptakeand/or transport, improving a plant's general transport mechanisms,assimilation pathway improvements, and the like), and/or by improvingspecific nutrient use efficiency of nutrients including, but not limitedto, phosphorus, potassium, and nitrogen.

According to the present invention, yield-related traits concerning animprovement or increase of stress tolerance of a plant may be manifestedby improving or increasing a plant's tolerance against stress,particularly abiotic stress. In the present application, abiotic stressrefers generally to abiotic environmental conditions a plant istypically confronted with, including conditions which are typicallyreferred to as “abiotic stress” conditions including, but not limitedto, drought (tolerance to drought may be achieved as a result ofimproved water use efficiency), heat, low temperatures and coldconditions (such as freezing and chilling conditions), salinity, osmoticstress, shade, high plant density, mechanical stress, oxidative stress,and the like.

According to the present invention, the improvement of yield-relatedtraits relating to an increase of the intrinsic yield capacity of aplant and/or to a plant's tolerance to abiotic stress(es) is aparticularly preferred embodiment for enhancing or improving yield ofsaid plant.

The term “yield” as used herein generally refers to a measurable producefrom a plant, particularly a crop.

Yield and yield increase (in comparison to a non-transformed starting orwild-type plant) can be measured in a number of ways, and it isunderstood that a skilled person will be able to apply the correctmeaning in view of the particular embodiments, the particular cropconcerned and the specific purpose or application concerned.

In the preferred embodiments of the present invention described herein,an increase in yield refers to increased biomass yield, increased seedyield, and/or increased yield regarding one or more specific content(s)of a whole plant or parts thereof or plant seed(s).

In preferred embodiments, “yield” refers to biomass yield comprising dryweight biomass yield and/or fresh weight biomass yield, each with regardto the aerial and/or underground parts of a plant, depending on thespecific circumstances (test conditions, specific crop of interest,application of interest, and the like). In each case, biomass yield maybe calculated as fresh weight, dry weight or a moisture adjusted basis,and on the other hand on a per plant basis or in relation to a specificarea (e.g. biomass yield per acre/square meter/or the like).

In other preferred embodiments, “yield” refers to seed yield which canbe measured by one or more of the following parameters: number of seedor number of filled seed (per plant or per area (acre/square meter orthe like)); seed filling rate (ratio between number of filled seeds andtotal number of seeds); number of flowers per plant; seed biomass ortotal seed weight (per plant or per area (acre/square meter or thelike); thousand kernel weight (TKW; extrapolated from the number offilled seeds counted and their total weight; an increase in TKW may becaused by an increased seed size, an increased seed weight, an increasedembryo size, and/or an increased endosperm); or other parametersallowing to measure seed yield. Seed yield may be determined on a dryweight or on a fresh weight basis, or typically on a moisture adjustedbasis, e.g. at 15.5 percent moisture.

In further preferred embodiments, yield refers to the specific contentand/or composition of a harvestable product, including, withoutlimitation, an enhanced and/or improved sugar content or sugarcomposition, an enhanced or improved starch content and/or starchcomposition, an enhanced and/or improved oil content and/or oilcomposition (such as enhanced seed oil content), an enhanced or improvedprotein content and/or protein composition (such as enhanced seedprotein content), an enhanced and/or improved vitamin content and/orvitamin composition, or the like.

In a preferred meaning according to the present application, “yield” asdescribed herein may also refer to the harvestable yield of a plant,which largely depends on the specific plant/crop of interest as well asits intended application (such as food production, feed production,processed food production, biofuel, biogas or alcohol production, or thelike) of interest in each particular case. Thus, yield may also becalculated as harvest index (expressed as a ratio of the weight of therespective harvestable parts divided by the total biomass), harvestableparts weight per area (acre, square meter, or the like); and the like.

Preferably, the preferred enhanced or improved yield characteristics ofa plant described herein according to the present invention can beachieved in the absence or presence of stress conditions.

The meaning of “yield” is, thus, mainly dependent on the crop ofinterest and the intended application, and it is understood, that theskilled person will understand in each particular case what is meantfrom the circumstances of the description.

In a preferred embodiment of the present invention, plant yield isincreased by increasing one or more of yield-related traits selectedfrom one or more improvements concerning the nutrient use efficiency ofa photosynthetic active organism, especially a plant. An improvement orincrease in nutrient use efficiency of a plant may be manifested byimproving a plant's general efficiency of nutrient assimilation (e.g. interms of improvement of general nutrient uptake and/or transport,improving a plant's general transport mechanisms, assimilation pathwayimprovements, and the like), and/or by improving specific nutrient useefficiency of nutrients including, but not limited to, phosphorus,potassium, and nitrogen.

The term “nutrient deficiency” refers to conditions where the respectivephotosynthetic organism, especially a plant, lacks of nutrient, likephosphorus, potassium or nitrogen; especially the term “nitrogendeficiency” refers to conditions where the respective photosyntheticorganism, especially a plant, lacks of or nitrogen.

In a preferred embodiment the present invention relates to themanipulation of the nitrogen use efficiency in photosynthetic activeorganisms, preferably in plants. In particular, the present inventionrelates to a process for the enhanced nitrogen uptake and/or nitrogenutilization, in photosynthetic active organisms, especially in plants.Also the present invention relates to a process for enhanced biomassproduction, especially under nitrogen limited conditions, inphotosynthetic active organisms, especially in plants.

In particular, this invention relates to plant cells and/or plantstailored to grow under conditions of nitrogen deficiency, and/or toplant cells and/or plants showing increased yield when grown undernon-nitrogen-deficiency conditions.

The invention also deals with methods of producing and screening for andbreeding such plant cells and/or plants.

Plant nutrition is essential to the growth and development of plants andtherefore also for quantity and quality of plant products. Because ofthe strong influence of the efficiency of nutrition uptake as well asnutrition utilization on plant yield and product quality, a huge amountof fertilizer is poured onto soils to optimize plant growth and quality.

Plant growth is primarily limited by three nutrients—phosphorous,potassium and nitrogen. Therefore nitrogen (N) is one of the majornutritional elements required for plant growth, which is usually therate-limiting element in plant growth. Nitrogen is part of numerousimportant compounds found in living cells, like amino acids, proteins(e.g. enzymes), nucleic acids, and chlorophyll. 1.5% to 2% of plant drymatter is nitrogen and approximately 16% of total plant protein. Thus,the availability of nitrogen has a major impact on amino acid synthesisas well as amino acid composition, accumulation of amino acids, onprotein synthesis and accumulation thereof, and based thereupon it is amajor limiting factor for plant growth and yield (Frink C.R., Proc.Natl. Acad. Sci. USA 96, 1175 (1999)).

Plants can utilize a wide range of nitrogen species including volatileammonia (NH₃), nitrogen oxides (NO_(x)), mineral nitrogen, like nitrate(NO₃ ⁻) and ammonium salts (NH₄ ⁺), urea and urea derivates, and organicnitrogen (amino acids, peptides, and the like). Some plants are able toutilize atmospheric nitrogen by symbiotic bacteria or certain fungi.However, in most agricultural soils, nitrate (NO₃ ⁻) is the mostimportant source of nitrogen (Crawford N.M., Glass A.D.M., Trends inPlant Science, 3 389 (1998); Hirsch R. E., Sussman M. R., TIBTech 17,356 (1999)). Nevertheless also ammonium NH₄ ⁺ plays an important,probably underestimated role, because most plants preferentially take upNH₄ ⁺ when both forms are present—even if NH₄ ⁺ is present at lowerconcentrations than NO₃ ⁻ (von Wiren N. et al., Curr. Opin. Plant Biol.3, 254 (2000)).

Because of the high nitrogen requirements for crop plants, nitrogenfertilization is a major worldwide agricultural investment, with 80million metric tons of nitrogen fertilizers (as nitrate and/or ammonium)applied annually (Frink C.R., Proc. Natl. Acad. Sci. USA 96, 1175(1999)). There are also negative environmental consequences for theextensive use of nitrogen containing fertilizers in crop productionsince the crops retain only about two-thirds of the applied nitrogen.Therefore high inputs of fertilizer are followed by large outputs byleaching, gaseous losses and crop removal. The unabsorbed nitrogen cansubsequently leach into the soil and contaminate water supplies (FrinkC.R., Proc. Natl. Acad. Sci. USA 96, 1175 (1999)). Because of the highleaching losses of nitrogen from agricultural ecosystems to surfacewater and groundwater, nitrogen is also recognized as a pollutant.Nitrogen leaching, namely as nitrate from agricultural lands, affectsdrinking water quality and causes eutrophication of lakes and coastalareas. Abundant use of nitrogen containing fertilizers can further leadto final deterioration of soil quality, to environmental pollution andhealth hazards.

Because of the high costs of nitrogen fertilizer in relation to therevenues for agricultural products, and additionally its deleteriouseffect on the environment, it is desirable to develop strategies toreduce nitrogen input and/or to optimize nitrogen uptake and/orutilization of a given nitrogen availability while simultaneouslymaintaining optimal yield, productivity and quality of photosyntheticactive organisms, preferably cultivated plants, e.g. crops. Also it isdesirable to obtain “existing” yield of crops with lower fertilizerinput and/or higher yield on soils of similar or even poorer quality.

For efficient nitrogen uptake and utilization, complex processesassociated with absorption, translocation, assimilation, andredistribution of nitrogen are required to operate effectively.Differences in nitrogen absorption between genotypes have beendemonstrated for several species by different researchers (Chang S. C.,Robison D. J., Sci. World J., Suppl. 2, 407 (2001)). Considerableevidence of genotypic differences in nitrogen uptake has also beenreported for maize and canola (Weisler et al., Sci. World J., Suppl. 2,61 (2001); Gallais A., Hirel B., J. Exper. Bot. 55, 295 (2004)).

Plants absorb nitrate via transporters localized to the root epidermaland cortical cell plasma membrane over a wide nitrate concentrationrange using several different transport mechanisms, includingconstitutive and nitrate-inducible high-affinity transport systems, aswell as nitrate-inducible low-affinity transporters (Stitt M., Curr.Opin. Plant Biol. 2, 178 (1999)). In addition nitrate uptake in plantsis highly regulated and coordinated with other transport and metabolicpathways (Crawford N.M. Plant Cell 7, 859 (1995)), and a number ofnitrate uptake and assimilation-related genes have been identified andcharacterized (Forde B.G., Ann. Rev. Plant Biol 53, 203 (2002)). Once inthe root cell cytoplasm, nitrate may be stored in the vacuole for lateruse, transported into the xylem and translocated to the shoot forassimilation and/or storage, released back into the rhizosphere, orreduced to nitrite and then to ammonia via nitrate reductase (NR) andnitrite reductases (NiR). The reduction of nitrate to nitrite and thento ammonia enables the assimilation of nitrogen into amino acids via theGOGAT pathway (Stitt M., Curr. Opin. Plant Biol. 2, 178 (1999)). Inorder to be incorporated into amino acids, nucleic acids, and othercompounds, NO₃ ⁻ must be reduced to NH₄ ⁺. NR (nitrate reductase) is thefirst enzyme in the process of NO₃ ⁻ reduction to NH₄ ⁺. It is asubstrate-inducible enzyme and is thought to be the most limiting stepin nitrogen assimilation.

The in-situ rate of NO₃ ⁻ reduction is controlled primarily by the rateof NO₃ ⁻ uptake, rather than by alterations in nitrate reductaseactivity (NRA) or limitations in reducing power. Thus, NO₃ ⁻ uptakeappears to be of primary importance in nitrogen assimilation in NO₃⁻-fed plants. Genetic variation in NRA is well documented in severalspecies. NRA is affected by factors such as environmental conditions andplant developmental stages, as well as plant part, such as roots andtops. Furthermore, in vivo and in vitro assays usually give differentresults. Variable results were found by several researchers in theirefforts to relate NRA to grain yield and N-related traits such as totalreduced plant nitrogen, grain nitrogen content, grain nitrogenconcentration, and nitrogen harvest index.

Beneath NO₃ ⁻ plants can take up nitrogen also in the form of ammonium.Although the average NH₄ ⁺ concentrations in soil are often 10 to 1000times lower than those of NO₃ ⁻ (Marschner H.L., “Mineral Nutrition inHigher Plants”, London, Academic Press, 1995), the difference in soilconcentrations does not necessarily reflect the uptake ratio of eachnitrogen source. Plants take up NH₄ ⁺ preferentially when both forms—NO₃⁻ as well as NH₄ ⁺—are available, possibly because its assimilationrequires less energy since NO₃ ⁻ has to be reduced prior to assimilation(Bloom et al., Plant Phys. 1294-1301 (1992)).

Ammonium uptake systems have been characterized in different organisms,including yeast and plants. The yeast Saccharomyces cerevisiae containsthree MEP genes for ammonium transporters, which are all controlled bynitrogen, being repressed in the presence of an nitrogen source that isreadily metabolized, such as NH₄ ⁺ (Marini et al., Mol. Cell. Biol. 17,4282 (1997)). Plant genes encoding ammonium transport systems have beencloned by complementation of a yeast mutant, homology searches indatabases and heterogonous hybridizations (von Wiren N. et al., Curr.Opin. Plant Biol., 3, 254 (2000)). Experimental evidence of thephysiological function of NH₄ ⁺ transporters mainly rely on correlationsbetween ammonium transporter expression and influx of labeled ammonium.The situation is complicated by the fact, that in Arabidopsis but alsoin other plants ammonium transporters are present in gene families, themembers of which have different expression patterns and physiologicalcharacteristics. Although DE 43 37 597 claims sequences for plantammonium transporters and their use for manipulation of the nitrogenmetabolism and plant growth under certain conditions, any evidence forpositive effects on nitrogen assimilation or plant growth under certainconditions through ectopic expression of the plant ammonium transportersare missing.

Usually the first step in the assimilation of inorganic nitrogen intoorganic form involves the reaction of glutamate with ammonium to formglutamine being catalyzed by glutamine synthase. Glutamine thus formedmay transfer in turn its amino function of the amido group to asparateto form asparagine being catalyzed by asparagine synthase. The steadyflow of nitrogen from ammonia to asparagine depends upon the recyclingof glutamate, alpha-ketogluterate and aspartate, being catalyzed byglutamine-2-oxoglutarate aminotransferase and aspartateaminotransferase. Glutamine and asparagine represent the major longdistance “nitrogen transport compounds” in plants. These are abundant inphloem sap but they have somewhat different roles in plant nitrogenmetabolism since glutamine is more metabolic active based on the factthat it can directly transfer its amino function of the amido group to anumber of substrates, whereas asparagine is more efficient in “nitrogentransport and storage”.

In order to describe the efficiency of the complete pathway of nitrogen,starting with the uptake from the soil, assimilation of nitrogen,transport and accumulation of N-containing compounds within thephotosynthetic organism, influencing biomass and yield, differentapproaches are known. And in the light of the importance of optimalnitrogen use different strategies have been followed for plantoptimizations.

In some cases enzymes of the nitrogen assimilation pathway, like ofglutamine synthetase, asparagine synthetase and asparaginase, wereoverexpressed. Although initially unsuccessful like the over-expressionof a cytosolic glutamine synthetase gene in Lotus (Vincent R. et al.,Planta 201, 424 (1997)), recent documents show at least some success. WO95/09911 describes the over-expression of glutamine-synthetase,asparagine-synthetase and asparaginase in transgenic plant forapplication in enhanced nitrogen-fixation and improved yield. Chichkovaet al. reported in J. Exp. Bot., 52, 2079 (2001) that transgenic tobaccoplants that overexpress alfalfa NADH-glutamate-synthase have highercarbon and nitrogen content, but not a specific enrichment in nitrogenin comparison to carbon. In another case, the over-expression of anitrogen assimilation gene, in this case the Escherichia coliglutamate-dehydrogenase, did not lead to a relative increase in nitrogencontent, but rather to a significant increase in fresh weight and dryweight. In another case, over-expression of the ASN1 gene enhances thenitrogen status in seeds of Arabidopsis (Lam H. et al., Plant Physiol.321, 926 (2003)). In seeds of those overexpressing lines the authorsobserved the elevation of soluble seed protein contents, elevation oftotal protein contents from acid-hydrolyzed seeds and a higher toleranceof young seedlings when grown under nitrogen-limiting conditions.

A different interesting approach was followed by Yanagisawa et al., PNAS101, 7833 (2004). The authors used hereby the transcription factor Dof1.The over-expression of this regulatory factor induced the up-regulationof genes encoding enzymes for carbon skeleton production, a markedincrease of amino acid contents, and a reduction of the glucose level intransgenic Arabidopsis. Elementary analysis revealed that the nitrogencontent increased in transgenic plants (approximate to 30%), indicatinga promotion of net nitrogen assimilation. Most significantly, the Dof1transgenic plants exhibit improved growth under low-nitrogen conditions.Although looking promising, this approach likely has the drawback, thatit relies on a plant transcription factor and the complex correspondingsignaling cascade which both might be the subject of different internalregulatory and feedback mechanism modifying or even diminishing thedesired effect at least under certain conditions.

Therefore, there is still a need for photosynthetic active organisms,especially plants, that are capable to use nitrogen more efficiently sothat less nitrogen is required for the same yield or higher yields maybe obtained with current levels of nitrogen use. In addition, there isstill a need for photosynthetic active organism, especially plants, thatshow an increase in biomass and/or yield.

Accordingly, it is also an object of this invention to develop aninexpensive process for an enhanced nitrogen up-take and/or transportand/or assimilation and/or utilisation in a photosynthetic activeorganism, which are reflected alone or altogether in an increasednitrogen use efficiency (NUE) and/or a process for an increased biomassproduction and/or yield under conditions of limited nitrogen supply.

It was found that this object is achieved by providing a processaccording to the present invention described herein.

It is further an object of this invention to provide plant cells and/orplants, which show an enhanced NUE, and/or exhibit under conditions oflimited nitrogen supply an increased biomass production and/or yield, ascompared to a corresponding non-transformed wild type plant cell and/orplant.

It was found that this object is achieved by providing plant cellsand/or plants according to the present invention described herein.

In one embodiment of the present invention, these traits are achieved bya process for the enhanced nitrogen utilization (=nitrogen useefficiency (NUE)) in a photosynthetic active organism, preferably aplant, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits a generallyenhanced yield (as defined hereinabove) under normal conditions or underlow nutrient conditions, especially an enhanced biomass yield per unitof nitrogen available from the surrounding medium, soil or environment,including nitrogen fertilizer, on which the photosynthetic activeorganism, preferably a plant, is grown, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhanceddry biomass yield per unit of nitrogen available from the surroundingmedium, soil or environment, including nitrogen fertilizer, on which thephotosynthetic active organism, preferably a plant, is grown, ascompared to a corresponding non-transformed wild type photosyntheticactive organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedaerial dry biomass yield per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedunderground dry biomass yield per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In another embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedfresh weight biomass yield per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedaerial fresh weight biomass yield per unit of nitrogen available fromthe surrounding medium, soil or environment, including nitrogenfertilizer, on which the photosynthetic active organism, preferably aplant, is grown, as compared to a corresponding non-transformed wildtype photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedunderground fresh weight biomass yield per unit of nitrogen availablefrom the surrounding medium, soil or environment, including nitrogenfertilizer, on which the photosynthetic active organism, preferably aplant, is grown, as compared to a corresponding non-transformed wildtype photosynthetic active organism.

In another embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of harvestable parts of a plant per unit of nitrogen availablefrom the surrounding medium, soil or environment, including nitrogenfertilizer, on which the photosynthetic active organism, preferably aplant, is grown, as compared to a corresponding non-transformed wildtype photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of dry harvestable parts of a plant per unit of nitrogen availablefrom the surrounding medium, soil or environment, including nitrogenfertilizer, on which the photosynthetic active organism, preferably aplant, is grown, as compared to a corresponding non-transformed wildtype photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of dry aerial harvestable parts of a plant per unit of nitrogenavailable from the surrounding medium, soil or environment, includingnitrogen fertilizer, on which the photosynthetic active organism,preferably a plant, is grown, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of underground dry harvestable parts of a plant per unit ofnitrogen available from the surrounding medium, soil or environment,including nitrogen fertilizer, on which the photosynthetic activeorganism, preferably a plant, is grown, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In another embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of fresh weight harvestable parts of a plant per unit of nitrogenavailable from the surrounding medium, soil or environment, includingnitrogen fertilizer, on which the photosynthetic active organism,preferably a plant, is grown, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of aerial fresh weight harvestable parts of a plant per unit ofnitrogen available from the surrounding medium, soil or environment,including nitrogen fertilizer, on which the photosynthetic activeorganism, preferably a plant, is grown, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of underground fresh weight harvestable parts of a plant per unitof nitrogen available from the surrounding medium, soil or environment,including nitrogen fertilizer, on which the photosynthetic activeorganism, preferably a plant, is grown, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In a further embodiment, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of the crop fruit per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of the fresh crop fruit per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of the dry crop fruit per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedgrain dry weight per unit of nitrogen supplied, as compared to acorresponding non-transformed wild type photosynthetic active organism,in analogy to Reynolds, M.P., Ortiz-Monasterioi J.J., and McNab A.(eds.), 2001, “Application of Physiology in Whaet Breeding, Mexico,D.F.:CIMMYT, which is incorporated by reference.

In a further embodiment, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of seeds per unit of nitrogen available from the surroundingmedium, soil or environment, including nitrogen fertilizer, on which thephotosynthetic active organism, preferably a plant, is grown, ascompared to a corresponding non-transformed wild type photosyntheticactive organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of fresh weight seeds per unit of nitrogen available from thesurrounding medium, soil or environment, including nitrogen fertilizer,on which the photosynthetic active organism, preferably a plant, isgrown, as compared to a corresponding non-transformed wild typephotosynthetic active organism.

In an embodiment thereof, the term “enhanced NUE” means that thephotosynthetic active organism, preferably a plant, exhibits an enhancedyield of dry seeds per unit of nitrogen available from the surroundingmedium, soil or environment, including nitrogen fertilizer, on which thephotosynthetic active organism, preferably a plant, is grown, ascompared to a corresponding non-transformed wild type photosyntheticactive organism.

In another embodiment of the present invention, these traits areachieved by a process for an increased biomass production and/or yieldunder conditions of limited nitrogen supply, in a photosynthetic activeorganism, preferably plant, as compared to a correspondingnon-transformed wild type photosynthetic active organism.

In an embodiment thereof, the term “increased biomass production” meansthat the photosynthetic active organism, especially a plant, exhibit anincreased growth rate under conditions of limited nitrogen supply,compared to the corresponding wild-type photosynthetic active organism.An increased growth rate may be reflected inter alia by an increasedbiomass production of the whole plant, or by an increased biomassproduction of the aerial parts of a plant, or by an increased biomassproduction of the underground parts of a plant, or by an increasedbiomass production of parts of a plant, like stems, leaves, blossoms,fruits, seeds.

In an embodiment thereof, increased biomass production includes higherfruit yields, higher seed yields, higher fresh matter production, and/orhigher dry matter production.

In another embodiment thereof, the term “increased biomass production”means that the photosynthetic active organism, preferably plant,exhibits a prolonged growth under conditions of limited nitrogen supply,as compared to the corresponding non-transformed wild typephotosynthetic active organism. A prolonged growth comprises survivaland/or continued growth of the photosynthetic active organism,preferably plant, at the moment when the non-transformed wild typephotosynthetic active organism shows visual symptoms of deficiencyand/or death.

In one embodiment of the invention the enhanced NUE is determinated andquantified according to the following method:

Transformed plants are grown in pots in a growth chamber (SvalöfWeibull, Svalöv, Sweden). In case the plants are Arabidopsis thalianaseeds thereof are sown in pots containing a 1:1 (v:v) mixture ofnutrient depleted soil (“Einheitserde Typ 0”, 30% clay, Tantau, WansdorfGermany) and sand. Germination is induced by a four day period at 4° C.,in the dark. Subsequently the plants are grown under standard growthconditions. In case the plants are Arabidopsis thaliana, the standardgrowth conditions are: photoperiod of 16 h light and 8 h dark, 20° C.,60% relative humidity, and a photon flux density of 200 μE/m²s. Plantsare grown and cultured. In case the plants are Arabidopsis thaliana theyare watered every second day with a N-depleted nutrient solution. TheN-depleted nutrient solution e.g. contains beneath water

mineral nutrient final concentration KCl 3.00 mM MgSO₄ × 7 H₂O 0.5 mMCaCl₂ × 6 H₂O 1.5 mM K₂SO₄ 1.5 mM NaH₂PO₄ 1.5 mM Fe-EDTA 40 μM H₃BO₃ 25μM MnSO₄ × H₂O 1 μM ZnSO₄ × 7 H₂O 0.5 μM Cu₂SO₄ × 5 H₂O 0.3 μM Na₂MoO₄ ×2 H₂O 0.05 μMbut no other N-containing salt.

After 9 to 10 days the plants are individualized. After a total time of29 to 31 days the plants are harvested and rated by the fresh weight ofthe aerial parts of the plants, preferably the rosettes.

In another embodiment of the present invention, plant yield is increasedby increasing one or more of yield-related traits selected from one ormore stress tolerance(s). During its life-cycle, a plant is generallyconfronted with a diversity of environmental conditions. Any suchconditions which may, under certain circumstances, have an impact onplant yield, are herein referred to as “stress” condition. Environmentalstresses may generally be divided into biotic and abiotic(environmental) stresses. For the sake of completeness, it is mentionedthat unfavorable nutrient conditions are sometimes also referred to as“environmental stress”. As will be appreciated by the skilled artisan,the present invention does also contemplate solutions for this kind ofenvironmental stress. This topic is described and dealt with in detailin the paragraphs hereinabove referring to increased nutrient useefficiency.

In a particularly preferred embodiment of the present invention,yield-related traits which can be improved by the present invention arestress tolerance(s).

In a preferred embodiment of the present invention, plant yield isincreased by increasing one or more of yield-related traits selectedfrom one or more abiotic stress tolerance(s).

Generally, the term “increased tolerance to stress” can be defined assurvival of plants, and/or higher yield production, under stressconditions as compared to a non-transformed wild type or starting plant.

For the purposes of the description of the present invention, the terms“enhanced tolerance to abiotic stress”, “enhanced resistance to abioticenvironmental stress”, “enhanced tolerance to environmental stress”,“improved adaptation to environmental stress” and other variations andexpressions similar in its meaning are used interchangeably and refer,without limitation, to an improvement in tolerance to one or moreabiotic environmental stress(es) as described herein and as compared toa corresponding (non-transformed) wild type (or starting) plant.

In a preferred embodiment of the present invention, plant yield isincreased by increasing one or more of yield-related traits selectedfrom one or more abiotic stress tolerance(s). In a particularlypreferred embodiment of the present invention, said yield-related traitis increased water use efficiency of a plant and/or increased toleranceto drought conditions.

Drought, heat, cold and salt stress have a common theme important forplant growth and that is water availability. Plants are typicallyexposed during their life cycle to conditions of reduced environmentalwater content. Most plants have evolved strategies to protect themselvesagainst these conditions of low water or desiccation. However, if theseverity and duration of the drought conditions are too great, theeffects on plant development, growth and yield of most crop plants areprofound. Continuous exposure to drought causes major alterations in theplant metabolism. These great changes in metabolism ultimately lead tocell death and consequently yield losses.

Developing stress-tolerant plants is a strategy that has the potentialto solve or mediate at least some of these problems (McKersie andLeshem, 1994. Stress and Stress Coping in Cultivated Plants, KluwerAcademic Publishers). However, traditional plant breeding strategies todevelop new lines of plants that exhibit resistance (tolerance) to thesetypes of stress are relatively slow and require specific resistant linesfor crossing with the desired line. Limited germplasm resources forstress tolerance and incompatibility in crosses between distantlyrelated plant species represent significant problems encountered inconventional breeding. Additionally, the cellular processes leading todrought, cold and salt tolerance and/or resistance are complex in natureand involve multiple mechanisms of cellular adaptation and numerousmetabolic pathways (McKersie and Leshem, 1994. Stress and Stress Copingin Cultivated Plants, Kluwer Academic Publishers). This multi-componentnature of stress tolerance and/or resistance has not only made breedingfor tolerance and/or resistance largely unsuccessful.

Plants are exposed during their life cycle also to heat, cold and saltstress. The protection strategies are similar to those of droughtresistance. Since high salt content in some soils results in lessavailable water for cell intake, its effect is similar to those observedunder drought conditions. Likewise, under freezing temperatures, plantcells loose water as a result of ice formation that starts in theapoplast and withdraws water from the symplast (McKersie and Leshem,1994. Stress and Stress Coping in Cultivated Plants, Kluwer AcademicPublishers). Physiologically these stresses are also interconnected andmay induce similar cellular damage. For example drought and salt stressare manifested primarily as osmotic stress, leading to the disruption ofhomeostasis and ion distribution in the cell (Serrano et al., 1999; Zhu,2001a; Wang et al., 2003). Oxidative stress, which frequentlyaccompanies high temperature, salinity or drought stress, may causedenaturation of functional or structural proteins (Smirnoff, 1998). As aconsequence these abiotic stresses often activate similar signalingpathways (Shinozaki and Ymaguchi-Shinozaki, 2000; Knight and Knight,2001; Zhu 2001b, 2002) and cellular responses, e.g. the production ofcertain stress proteins, anti-oxidants and compatible solutes (Vierlingand Kimpel, 1992; Zhu et al., 1997; Cushman and Bohnert, 2000).

At the moment many genetical and biotechnological approaches are knownin order to obtain plants growing under conditions of low wateravailability.

These approaches are generally based on the introduction and expressionof genes in plant cell coding for different enzymes as disclosed forexample in WO 2004/011888, WO 2006.032708, US 20050097640, US20060037108, US 20050108791, Serrano et al. (Scientia Horticulturae 78,261-269 (1999)) and many others.

For example the over-expression of antioxidant enzymes or ROS-scavengingenzymes is one possibility to engineer tolerance, e.g. transgenicalfalfa plants expressing Mn-superoxide dismutase tend to have reducedinjury after water-deficit stress (McKersie et al., Plant Physiol. 111,1177-1181 (1996)). These same transgenic plants have increased biomassproduction in field trials (McKersie et al., Plant Physiology 119,839-847 (1999); McKersie et al., Plant Physiol. 111, 1177-1181 (1996)).Transgenic plants that overproduce osmolytes such as mannitol, fructans,proline or glycine-betaine also show increased resistance to some formsof abiotic stress and it is proposed that the synthesized osmolytes actas ROS scavengers (Tarczynski. et al. Science 259, 508-510 (1993);Sheveleva, et al., Plant Physiol. 115, 1211-1219 (1997)).

Generally the transformed and stress resistant plants cited exhibitslower growth and reduced biomass, due to an imbalance in developmentand physiology of the plant, thus having significant fitness cost(Kasuga et al., 1999, Danby and Gehring et al., 2005). Despitemaintaining basic metabolic function this leads to severe biomass andyield loss. Sometimes the root/shoot dry weight ratio increases as plantwater stress develops. The increase is mostly due to a relativereduction in shoot dry weight. The ratio of seed yield to above-grounddry weight is relatively stable under many environmental conditions andso a robust correlation between plant size and grain yield can often beobtained. These processes are intrinsically linked because the majorityof grain biomass is dependent on current stored photosyntheticproductivity by the leaves and stem of the plant. Therefore selectingfor plant size, even at early stages of development, has been used as anindicator for future potential.

In some cases (US 20060037108) an increased biomass, mainly a greatershoot biomass was observed after a drought treatment by withholdingwater for 6 to 8 days.

There is still a need to identify genes expressed in stress tolerantplants that have the capacity to confer stress resistance to its hostplant and to other plant species, especially to confer increasedtolerance and/or resistance to environmental stress, preferably underconditions of water deficiency and confers increased biomass production.

It is an object of this invention to identify new methods to conferstress tolerance and/or resistance in plants or plant cells.

In preferred embodiments of the present invention, thus, abioticenvironmental stress refers to drought and low water content, whereindrought stress means any environmental stress which leads to a lack ofwater in plants or reduction of water supply to plants, includingdesiccation.

In a further embodiment of the invention the term “increased toleranceto abiotic stress” relates to an increased tolerance to water stress,which is produced as a secondary stress by low temperature and/or salt,and/or as a primary stress during drought or heat.

In accordance with the present invention, in one embodiment, increasedtolerance to drought conditions can be determinated and quantifiedaccording to the following method:

Transformed plants are grown individually in pots in a growth chamber(York Industriekälte GmbH, Mannheim, Germany). Germination is induced.In case the plants are Arabidopsis thaliana sown seeds are kept at 4°C., in the dark, for 3 days in order to induce germination. Subsequentlyconditions are changed for 3 days to 20° C./6° C. day/night temperaturewith a 16/8 h day-night cycle at 150 μE. Subsequently the plants aregrown under standard growth conditions. In case the plants areArabidopsis thaliana, the standard growth conditions are: photoperiod of16 h light and 8 h dark, 20° C., 60% relative humidity, and a photonflux density of 200 μE. Plants are grown and cultured until they developleaves. In case the plants are Arabidopsis thaliana they are watereddaily until they were approximately 3 weeks old. Starting at that timedrought was imposed by withholding water. After the non-transformed wildtype plants show visual symptoms of injury, the evaluation starts andplants are scored for symptoms of drought symptoms and biomassproduction comparison to wild type and neighboring plants for 5-6 daysin succession.

Visual symptoms of injury stating for one or any combination of two,three or more of the following features:

-   a) wilting-   b) leaf browning-   c) loss of turgor, which results in drooping of leaves or needles    stems, and flowers,-   d) drooping and/or shedding of leaves or needles,-   e) the leaves are green but leaf angled slightly toward the ground    compared with controls,-   f) leaf blades begun to fold (curl) inward,-   g) premature senescence of leaves or needles,-   h) loss of chlorophyll in leaves or needles and/or yellowing.

In another preferred embodiment of the present invention, plant yield isincreased by increasing one or more of yield-related traits selectedfrom one or more abiotic stress tolerance(s). In a particularlypreferred embodiment of the present invention, said yield-related traitis increased tolerance to heat conditions.

In a preferred embodiment of the present invention, plant yield isincreased by increasing one or more of yield-related traits selectedfrom one or more abiotic stress tolerance(s). In a particularlypreferred embodiment of the present invention, said yield-related traitis increased low temperature tolerance, comprising freezing toleranceand/or chilling tolerance.

Environmental temperatures change within minutes to hours in the diurnalcycle, in hours to days as a result of changing weather, and over weeksto months as a result of seasonal changes. Low temperatures impinge on aplethora of biological processes. They retard or inhibit almost allmetabolic and cellular processes, with the typical Q10 forprotein-dependent catalysis lying between 2 and 3. They impact onmembrane-based processes, because low temperatures alter the physicalproperties of lipids and reduce membrane fluidity. At temperatures belowzero, there is the additional danger of ice formation. This typicallytakes place in the apoplast of a cell, leading to withdrawal of waterand dehydration of the symplast. The response of plants to lowtemperature is an important determinant of their ecological range. Theproblem of coping with low temperatures is exacerbated by the need toprolong the growing season beyond the short summer found at highlatitudes or altitudes.

Most plants have evolved adaptive strategies to protect themselvesagainst low temperatures. Generally, adaptation to low temperature maybe divided into chilling tolerance, and freezing tolerance.

Chilling tolerance is naturally found in species from temperate orboreal zones and allows survival and an enhanced growth at low butnon-freezing temperatures. Species from tropical or subtropical zonesare chilling sensitive and often show wilting, chlorosis or necrosis,slowed growth and even death at temperatures around 10° C. during one ormore stages of development. Freezing tolerance allows survival at nearzero to particularly subzero temperatures. It is believed to be promotedby a process termed cold-acclimation which occurs at low butnon-freezing temperatures and provides increased freezing tolerance atsubzero temperatures. In addition, most species from temperate regionshave life cycles that are adapted to seasonal changes of thetemperature. For those plants, low temperatures may also play animportant role in plant development through the process ofstratification and vernalisation. It becomes obvious that a clearcutdistinction between or definition of chilling tolerance and freezingtolerance is difficult and that the processes may be overlapping orinterconnected.

The molecular basis of freezing tolerance has been intensivelyresearched in Arabidopsis. Physiological changes during cold acclimationinclude changes in lipid composition to increase membrane fluidity,expression of proteins that modify the physical characteristics ofmembranes, accumulation of compatible solutes like sucrose, raffinoseand proline (Cook et al., Proc. Natl. Acad. Sci. USA 101, 15243-15248(2004)), detoxification of active oxygen species and altered leafdevelopment to increase the levels of proteins involved inphotosynthetic electron transport and carbon fixation. Some of thesechanges are specific for low temperature, and others also occur inresponse to dehydration, mechanical stress.

Less is known about the molecular basis of chilling tolerance atdifferent stages of plant development. Exposure of chilling-sensitivespecies to low temperatures has a negative impact on seed germinationrates as well as early seedling growth and interferes withphotosynthesis of the growing plant which may result in photoinhibition.In particular, the process of seed germination strongly depends onenvironmental temperature and the properties of the seeds determine thelevel of activity and performance during germination and seedlingemergence when being exposed to low temperature. Chilling often delaysleaf development and interferes with plastid biogenesis, leading todelayed greening, chlorosis and thickening or deformation of new leaves.Chilling temperatures inhibit respiration, phloem transport, andrestrict the utilization of photoassimilate for growth. As one result,sugars and other metabolites accumulate and cause osmotic imbalance.

Chilling tolerance is a major breeding trait because most major crops,particularly corn (maize), bean, rice, soy bean, cotton, tomato, banana,cucumber and potato, are chilling-sensitive.

Breeding of crops with improved adaption to abiotic environmentalstresses, and particularly low temperature (i.e. chilling toleranceand/or freezing tolerance), will result in a better trait for stresstolerance and is expected to increase quality and yield of therespective crop. However, the genetic and molecular basis of chillingresponses is poorly understood. Although genetic diversity has beenidentified, for example from landraces and related species that grow atlight altitudes, and is being introduced into breeding lines, the genesresponsible for the qualitative trait loci have not yet been identified.Additionally, it becomes evident that stress tolerance in plants likelow temperature, drought, heat and salt stress tolerance have a commontheme important for plant growth, namely the availability of water.Plants are typically exposed during their life cycle to conditions ofreduced environmental water content.

The protection strategies are similar to those of chilling tolerance.For example components of low temperature, drought, heat and salt stressare manifested as osmotic stress, leading to the disruption ofhomeostasis and ion distribution in the cell (Serrano et al., J Exp Bot50, 1023-1036 (1999); Zhu J.K. Trends Plant Sci 6, 66-71 (2001a); Wanget al., 2003). Under freezing temperatures, plant cells loose water as aresult of ice formation that starts in the apoplast and withdraws waterfrom the symplast (McKersie and Leshem, 1994. Stress and Stress Copingin Cultivated Plants, Kluwer Academic Publishers). Oxidative stress,which frequently accompanies low/high temperature, salinity or droughtstress, may cause denaturation of functional or structural proteins(Smirnoff, Curr. Opin. Biotech. 9, 214-219 (1998)). As a consequencethese abiotic stresses often activate similar signaling pathways(Shinozaki and Ymaguchi-Shinozaki, 2000; Knight and Knight, 2001; ZhuJ.K. Curr.Opin Plant Biol. 4, 401-406 (2001b), Zhu, Annu. Rev. PlantBiol. 53, 247-73 (2002)) and cellular responses, e.g. the production ofcertain stress proteins, anti-oxidants and compatible solutes (Vierlingand Kimpel, 1992; Zhu et al., 1997; Cushman and Bohnert, 2000). Forexample, heat stress shares transcriptional responses that are similarto response pathways induced by other abiotic stresses (e.g. Swindell etal., BMC Genomics, 8,125 (2007)).

Developing stress-tolerant and/or resistant plants, particularly lowtemperature tolerant and/or resistant plants, is a strategy that has thepotential to solve or mediate at least some of the existing problems(McKersie and Leshem, 1994. Stress and Stress Coping in CultivatedPlants, Kluwer Academic Publishers). However, traditional plant breedingstrategies to develop new lines of plants that exhibit tolerance tothese types of stress are relatively slow and require specific resistantlines for crossing with the desired line. Limited germplasm resourcesfor stress tolerance and incompatibility in crosses between distantlyrelated plant species represent significant problems encountered inconventional breeding.

Additionally, the cellular processes leading to drought, low temperatureand salt tolerance are complex in nature and involve multiple mechanismsof cellular adaptation and numerous metabolic pathways (McKersie andLeshem, 1994. Stress and Stress Coping in Cultivated Plants, KluwerAcademic Publishers). This multi-component nature of stress tolerancehas not only made breeding for tolerance largely unsuccessful, but hasalso limited the ability to genetically engineer stress tolerance plantsusing biotechnological methods.

The results of current research indicate that tolerance to lowtemperature is a complex quantitative trait. The lack of a mechanisticunderstanding makes it difficult to design a transgenic approach toimprove stress tolerance.

At the time the invention was made, a couple of genetical andbiotechnological approaches are known in order to obtain plants growingunder conditions of low temperature. These approaches are generallybased on the introduction and expression of genes in plant cells codingfor different enzymes, as disclosed for example in WO 2007/044988, WO2007/078280, WO 1992/013082, WO 2007/052376, WO 2006/137574.

The over-expression of antioxidant enzymes or ROS-scavenging enzymes isone possibility to engineer tolerance, e.g. transgenic alfalfa plantsexpressing Mn-superoxide dismutase tend to have reduced injury afterwater-deficit stress (McKersie et al., Plant Physiol. 111, 1177-1181(1996)). These same transgenic plants show increased yield in fieldtrials (McKersie et al., 1999. Plant Physiology, 119, 839-847 (1999);McKersie et al., Plant Physiol. 111, 1177-1181 (1996)). Transgenicplants that overproduce osmolytes such as mannitol, fructans, proline orglycine-betaine also show increased tolerance to some forms of abioticstress and it is proposed that the synthesized osmolytes act as ROSscavengers (Tarczynski et al., Science 259, 508-510 (1993); Sheveleva,et al., Plant Physiol. 115, 1211-1219 (1997)).

Nevertheless, the transformed and stress resistant plants cited abovegenerally exhibit slower growth and reduced biomass, due to an imbalancein development and physiology of the plant, thus having significantfitness cost (Kasuga et al., Nature Biotech 17, 287-291 (1999)). Despitemaintaining basic metabolic function this leads to severe biomass andyield loss. Sometimes the root/shoot dry weight ratio increase as plantwater stress develops. The increase is mostly due to a relativereduction in shoot dry weight. The ratio of seed yield to above-grounddry weight is relatively stable under many environmental conditions andso a robust correlation between plant size and grain yield can often beobtained. These processes are intrinsically linked because the majorityof grain biomass is dependent on current stored photosyntheticproductivity by the leaves and stem of the plant. Therefore selectingfor plant size, even at early stages of development, has been used as anindicator for future yield potential.

Accordingly, for the purposes of the description of the presentinvention, improved or enhanced “chilling tolerance” or variationsthereof refers to improved adaptation to low but non-freezingtemperatures around 10° C., preferably temperatures between 1 to 18° C.,more preferably 4-14° C., and most preferred 8 to 12° C.; hereinaftercalled “chilling temperature.

For the purposes of the description of the present invention, improvedor enhanced “freezing tolerance” or variations thereof refers toimproved adaptation to temperatures near or below zero, namelypreferably temperatures below 4° C., more preferably below 3 or 2° C.,and particularly preferred at or below 0 (zero)° C. or below −4° C., oreven extremely low temperatures down to −10° C. or lower; hereinaftercalled “freezing temperature.

More generally, “improved adaptation” to environmental stress like e.g.freezing and/or chilling temperatures refers to an improved plantperformance, while plant performance refers to more yield, particularlywith regard to one or more of the yield related traits as defined inmore detail above.

Accordingly, for the purposes of the description of the presentinvention, the term “low temperature” with respect to low temperaturestress on a plant, and preferably a crop plant, refers to any of the lowtemperature conditions as described herein, preferably chilling and/orfreezing temperatures as defined above, as the context requires. It isunderstood that a skilled artisan will be able to recognize from theparticular context in the present description which temperature ortemperature range is meant by “low temperature”.

In the present invention, enhanced tolerance to low temperature may, forexample and preferably, be determined according to the following method:

Transformed plants are grown in pots in a growth chamber (e.g. York,Mannheim, Germany). In case the plants are Arabidopsis thaliana seedsthereof are sown in pots containing a 3.5:1 (v:v) mixture of nutrientrich soil (GS90, Tantau, Wansdorf, Germany) and sand. Plants are grownunder standard growth conditions. In case the plants are Arabidopsisthaliana, the standard growth conditions are: photoperiod of 16 h lightand 8 h dark, 20° C., 60% relative humidity, and a photon flux densityof 200 μmol/m²s. Plants are grown and cultured. In case the plants areArabidopsis thaliana they are watered every second day. After 9 to 10days the plants are individualized. Cold (e.g. chilling at 11-12° C.) isapplied 14 days after sowing until the end of the experiment. After atotal growth period of 29 to 31 days the plants are harvested and ratedby the fresh weight of the aerial parts of the plants, in the case ofArabidopsis preferably the rosettes.

In another preferred embodiment of the present invention, plant yield isincreased by increasing one or more of yield-related traits selectedfrom one or more abiotic stress tolerance(s). In a particularlypreferred embodiment of the present invention, said yield-related traitmay also be increased salinity tolerance (salt tolerance), tolerance toosmotic stress, increased shade tolerance, increased tolerance to a highplant density, increased tolerance to mechanical stresses, and/orincreased tolerance to oxidative stress.

In another preferred embodiment of the present invention, plant yield isincreased by increasing yield in the absence of stress as well as theabsence of nutrient deficiencies (=intrinsic yield).

Accordingly, in preferred embodiments, the present invention provides amethod for producing a transgenic plant cell nucleus; a transgenic plantcell; plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing increased yield as compared toa corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,61267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, the presentinvention provides a transgenic plant cell nucleus; a transgenic plantcell; plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing increased yield as compared toa corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

In the preferred embodiments of the present invention, yield isincreased by improving one or more of the yield-related traits asdefined herein.

Accordingly, in an embodiment, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nutrient useefficiency as compared to a corresponding non-transformed wild typeplant cell or plant, especially a transgenic plant cell and/or plantwith increased NUE and/or increased biomass production as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in particularlypreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nutrient use efficiency as compared to a correspondingnon-transformed wild type plant cell or plant, especially a transgenicplant cell and/or plant with increased NUE and/or increased biomassproduction as compared to a corresponding non-transformed wild typeplant cell or plant, by increasing or generating one or more activitiesselected from the group consisting of 2-dehydro-3-deoxy-phosphoheptonatealdolase, 3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

In other particularly preferred embodiments, the present inventionprovides a method for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nutrient use efficiency, especially a transgenic plant celland/or plant with increased NUE and/or increased biomass production, andan increased stress resistance, particularly abiotic stress resistance,especially an increased low temperature tolerance, in particular anincreased tolerance to chilling, and/or an increased water useefficiency, in particular tolerance to drought conditions, as comparedto a corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such otherparticularly preferred embodiments, the present invention provides atransgenic plant cell nucleus; a transgenic plant cell; plant(s)comprising one or more of such transgenic nuclei or plant cell(s);progeny, seed, and/or pollen derived from such plant cell and/ortransgenic plant(s); each showing an increased nutrient use efficiency,especially a transgenic plant cell and/or plant with increased NUEand/or increased biomass production, and increased stress resistance,particularly abiotic stress resistance, especially an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and/or an increased water use efficiency, in particular tolerance todrought conditions, as compared to a corresponding non-transformed wildtype plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Thus, in the most preferred embodiments of the present invention, amethod is provided for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nitrogen use efficiency (NUE) and an increased low temperaturetolerance, particularly chilling tolerance, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such mostpreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nitrogen use efficiency (NUE) and an increased low temperaturetolerance, particularly chilling tolerance, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Thus, in the most preferred embodiments of the present invention, amethod is provided for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nitrogen use efficiency (NUE) and an increased water useefficiency, particularly tolerance to drought conditions, as compared toa corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such mostpreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nitrogen use efficiency (NUE) and an increased water useefficiency (WUE) particularly tolerance to drought conditions, ascompared to a corresponding non-transformed wild type plant cell orplant, by increasing or generating one or more activities selected fromthe group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Thus, in the most preferred embodiments of the present invention, amethod is provided for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nitrogen use efficiency (NUE), an increased low temperaturetolerance, particularly chilling tolerance, and an increased water useefficiency, particularly tolerance to drought conditions, as compared toa corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such mostpreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nitrogen use efficiency (NUE), an increased low temperaturetolerance, particularly chilling tolerance and an increased water useefficiency (WUE) particularly tolerance to drought conditions, ascompared to a corresponding non-transformed wild type plant cell orplant, by increasing or generating one or more activities selected fromthe group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Accordingly, in an embodiment, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nutrient useefficiency as compared to a corresponding non-transformed wild typeplant cell or plant, especially a transgenic plant cell and/or plantwith increased NUE and/or increased biomass production as compared to acorresponding non-transformed wild type plant cell or plant, andincreased yield in the absence of stress as well as the absence ofnutrient deficiencies, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, 61258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in particularlypreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nutrient use efficiency as compared to a correspondingnon-transformed wild type plant cell or plant, especially a transgenicplant cell and/or plant with increased NUE and/or increased biomassproduction as compared to a corresponding non-transformed wild typeplant cell or plant, and increased yield in the absence of stress aswell as the absence of nutrient deficiencies, by increasing orgenerating one or more activities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

In other particularly preferred embodiments, the present inventionprovides a method for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nutrient use efficiency, especially a transgenic plant celland/or plant with increased NUE and/or increased biomass production, andan increased stress resistance, particularly abiotic stress resistance,especially an increased low temperature tolerance, in particular anincreased tolerance to chilling, and/or an increased water useefficiency, in particular tolerance to drought conditions, and increasedyield in the absence of stress as well as the absence of nutrientdeficiencies, as compared to a corresponding non-transformed wild typeplant cell or plant, by increasing or generating one or more activitiesselected from the group consisting of 2-dehydro-3-deoxy-phosphoheptonatealdolase, 3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such otherparticularly preferred embodiments, the present invention provides atransgenic plant cell nucleus; a transgenic plant cell; plant(s)comprising one or more of such transgenic nuclei or plant cell(s);progeny, seed, and/or pollen derived from such plant cell and/ortransgenic plant(s); each showing an increased nutrient use efficiency,especially a transgenic plant cell and/or plant with increased NUEand/or increased biomass production, and an increased stress resistance,particularly abiotic stress resistance, especially an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and/or an increased water use efficiency, in particular tolerance todrought conditions, and increased yield in the absence of stress as wellas the absence of nutrient deficiencies, as compared to a correspondingnon-transformed wild type plant cell or plant, by increasing orgenerating one or more activities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Thus, in the most preferred embodiments of the present invention, amethod is provided for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nitrogen use efficiency (NUE) and increased yield, in theabsence of stress as well as the absence of nutrient deficiencies, andan increased low temperature tolerance, particularly chilling tolerance,as compared to a corresponding non-transformed wild type plant cell orplant, by increasing or generating one or more activities selected fromthe group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such mostpreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nitrogen use efficiency (NUE) and increased yield, in theabsence of stress as well as the absence of nutrient deficiencies, andan increased low temperature tolerance, particularly chilling tolerance,as compared to a corresponding non-transformed wild type plant cell orplant, by increasing or generating one or more activities selected fromthe group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Thus, in the most preferred embodiments of the present invention, amethod is provided for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nitrogen use efficiency (NUE) and increased yield, in theabsence of stress as well as the absence of nutrient deficiencies, andan increased water use efficiency, particularly tolerance to droughtconditions, as compared to a corresponding non-transformed wild typeplant cell or plant, by increasing or generating one or more activitiesselected from the group consisting of 2-dehydro-3-deoxy-phosphoheptonatealdolase, 3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such mostpreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nitrogen use efficiency (NUE) and increased yield, in theabsence of stress as well as the absence of nutrient deficiencies, andan increased water use efficiency (WUE) particularly tolerance todrought conditions, as compared to a corresponding non-transformed wildtype plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Thus, in the most preferredembodiments of the present invention, a method is provided for producinga transgenic plant cell nucleus; a transgenic plant cell; plant(s)comprising one or more of such transgenic nuclei or plant cell(s);progeny, seed, and/or pollen derived from such plant cell and/ortransgenic plant(s); each showing an increased nitrogen use efficiency(NUE), an increased yield, in the absence of stress as well as theabsence of nutrient deficiencies, an increased low temperaturetolerance, particularly chilling tolerance, and an increased water useefficiency, particularly tolerance to drought conditions, as compared toa corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. Furthermore, in such mostpreferred embodiments, the present invention provides a transgenic plantcell nucleus; a transgenic plant cell; plant(s) comprising one or moreof such transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showingincreased nitrogen use efficiency (NUE), an increased yield in theabsence of stress as well as the absence of nutrient deficiencies, anincreased low temperature tolerance, particularly chilling tolerance andan increased water use efficiency (WUE) particularly tolerance todrought conditions, as compared to a corresponding non-transformed wildtype plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Among these particularly preferred embodiments of the present invention,the preferred increased nutrient use efficiency achieved in accordancewith the methods of the present invention, and shown by the transgenicplant cell nucleus; a transgenic plant cell; plant(s) comprising one ormore of such transgenic nuclei or plant cell(s); progeny, seed, and/orpollen derived from such plant cell and/or transgenic plant(s), whichare provided by the present invention, is increased nitrogen useefficiency (NUE).

In the preferred embodiments of the present invention described above,it is even more preferred the increase or generation of one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease is effected by one or morenucleic acid sequences as shown in table I, column 5 or 7, by one ormore proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

For the purpose of the description of the present invention the proteinshaving an activity selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, polypeptides encoded by one ormore nucleic acid sequences encoded by one or more nucleic acidsequences as shown in table I, column 5 or 7, and/or the polypeptides asdepicted in table II, application no. 1, column 5 or 7 are named as “NUErelated protein” NUERP.

Thus, in preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing increased yield as compared toa corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, the present invention provides atransgenic plant cell nucleus; a transgenic plant cell; plant(s)comprising one or more of such transgenic nuclei or plant cell(s);progeny, seed, and/or pollen derived from such plant cell and/ortransgenic plant(s); each showing increased yield as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In these preferred embodiments of the present invention, yield isincreased by improving one or more of the yield-related traits asdefined herein.

Thus, in particularly preferred embodiments, the present inventionprovides a method for producing a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing anincreased nutrient use efficiency as compared to a correspondingnon-transformed wild type plant cell or plant, by increasing orgenerating one or more activities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in particularly preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednutrient use efficiency as compared to a corresponding non-transformedwild type plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased NUE and/orincreased biomass production, and an increased stress resistance,particularly abiotic stress resistance, especially an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and/or an increased water use efficiency, in particular tolerance todrought conditions, as compared to a corresponding non-transformed wildtype plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such other particularly preferredembodiments, the present invention provides a transgenic plant cellnucleus; a transgenic plant cell; plant(s) comprising one or more ofsuch transgenic nuclei or plant cell(s); progeny, seed, and/or pollenderived from such plant cell and/or transgenic plant(s); each showing anincreased NUE and/or increased biomass production, and an increasedstress resistance, particularly abiotic stress resistance, especially anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and/or an increased water use efficiency, inparticular tolerance to drought conditions, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nitrogen useefficiency and an increased low temperature resistance, particularlychilling tolerance, as compared to a corresponding non-transformed wildtype plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednitrogen use efficiency and an increased low temperature tolerance,particularly chilling tolerance, as compared to a correspondingnon-transformed wild type plant cell or plant, by increasing orgenerating one or more activities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, 62646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nitrogen useefficiency and an increased water use efficiency, particularly toleranceto drought conditions, as compared to a corresponding non-transformedwild type plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, 62646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednitrogen use efficiency and an increased water use efficiency,particularly tolerance to drought conditions, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nitrogen useefficiency and an increased low temperature resistance, particularlychilling tolerance, and an increased water use efficiency, particularlytolerance to drought conditions, as compared to a correspondingnon-transformed wild type plant cell or plant, by increasing orgenerating one or more activities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednitrogen use efficiency and an increased low temperature tolerance,particularly chilling tolerance, and an increased water use efficiency,particularly tolerance to drought conditions, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nutrientefficiency, especially an increased nitrogen use efficiency and/orincreased biomass production, and increased yield in the absence ofstress as well as the absence of nutrient deficiencies, as compared tothe corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednutrient efficiency, especially increased nitrogen use efficiency and/orincreased biomass production, and an increased in the absence of stressas well as the absence of nutrient deficiencies, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nutrientefficiency, especially an increased nitrogen use efficiency and/orincreased biomass production, and increased yield in the absence ofstress as well as the absence of nutrient deficiencies, as compared tothe corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednutrient efficiency, especially increased nitrogen use efficiency and/orincreased biomass production, and an increased yield in the absence ofstress as well as the absence of nutrient deficiencies, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nutrientefficiency, especially an increased nitrogen use efficiency and/orincreased biomass production, and an increased stress resistance,particularly abiotic stress resistance, especially an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and/or an increased water use efficiency, in particular tolerance todrought conditions, and increased yield in the absence of stress as wellas the absence of nutrient deficiencies, as compared to thecorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednutrient efficiency, especially increased nitrogen use efficiency and/orincreased biomass production, and an increased stress resistance,particular abiotic stress resistance, especially low temperaturetolerance, in particular tolerance to chilling, and/or an increasedwater use efficiency, in particular tolerance to drought conditions, andan increased yield in the absence of stress as well as the absence ofnutrient deficiencies, as compared to a corresponding non-transformedwild type plant cell or plant, by increasing or generating one or moreactivities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nitrogen useefficiency and increased yield in the absence of stress as well as theabsence of nutrient deficiencies, and an increased low temperaturetolerance, particularly chilling tolerance, as compared to thecorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednitrogen use efficiency and an increased yield in the absence of stressas well as the absence of nutrient deficiencies, and an increased lowtemperature tolerance, particularly chilling tolerance, as compared to acorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nitrogen useefficiency and increased yield in the absence of stress as well as theabsence of nutrient deficiencies, and an increased water use efficiency,particularly tolerance to drought conditions, as compared to thecorresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednitrogen use efficiency and an increased yield in the absence of stressas well as the absence of nutrient deficiencies, and an increased wateruse efficiency, particularly tolerance to drought conditions, ascompared to a corresponding non-transformed wild type plant cell orplant, by increasing or generating one or more activities selected fromthe group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In other preferred embodiments, the present invention provides a methodfor producing a transgenic plant cell nucleus; a transgenic plant cell;plant(s) comprising one or more of such transgenic nuclei or plantcell(s); progeny, seed, and/or pollen derived from such plant celland/or transgenic plant(s); each showing an increased nitrogen useefficiency, increased yield in the absence of stress as well as theabsence of nutrient deficiencies, an increased low temperaturetolerance, particularly chilling tolerance, and an increased water useefficiency, particularly tolerance to drought conditions, as compared tothe corresponding non-transformed wild type plant cell or plant, byincreasing or generating one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7. Furthermore, in such even more preferred embodiments,the present invention provides a transgenic plant cell nucleus; atransgenic plant cell; plant(s) comprising one or more of suchtransgenic nuclei or plant cell(s); progeny, seed, and/or pollen derivedfrom such plant cell and/or transgenic plant(s); each showing increasednitrogen use efficiency, an increased yield in the absence of stress aswell as the absence of nutrient deficiencies, an increased lowtemperature tolerance, particularly chilling tolerance, and an increasedwater use efficiency, particularly tolerance to drought conditions, ascompared to a corresponding non-transformed wild type plant cell orplant, by increasing or generating one or more activities selected fromthe group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,3-keto sterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease, which is effected by one ormore nucleic acid sequences as shown in table I, column 5 or 7, by oneor more proteins each comprising a polypeptide encoded by one or morenucleic acid sequences as shown in table I, column 5 or 7, and/or by oneor more protein(s) each comprising a polypeptide as depicted in tableII, column 5 or 7.

In a preferred embodiment of the invention a photosynthetic activeorganism, especially a plant, shows an enhanced NUE.

In another preferred embodiment a photosynthetic active organism,especially a plant, shows increased biomass production and/or yieldunder conditions of limited nitrogen supply.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased yield in a plant uponexpression or over-expression of endogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased yield in aplant upon expression or over-expression of one or more endogenousgenes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased yield in aplant upon expression or over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased nutrient efficiency,especially an increased NUE, and an increased stress resistance,particularly abiotic stress resistance, especially an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and/or an increased water use efficiency, in particular tolerance todrought conditions, in a plant upon expression or over-expression ofendogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased nutrientefficiency, especially an increased NUE, and an increased stressresistance, particularly abiotic stress resistance, especially anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and/or an increased water use efficiency, inparticular tolerance to drought conditions, in a plant upon expressionor over-expression of one or more endogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased nutrientefficiency, especially an increased NUE, and an increased stressresistance, particularly abiotic stress resistance, especially anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and/or an increased water use efficiency, inparticular tolerance to drought conditions, in a plant upon expressionor over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased NUE, and an increased lowtemperature tolerance, in particular an increased tolerance to chilling,in a plant upon expression or over-expression of endogenous and/orexogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, and anincreased low temperature tolerance, in particular an increasedtolerance to chilling, in a plant upon expression or over-expression ofone or more endogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, and anincreased low temperature tolerance, in particular an increasedtolerance to chilling, in a plant upon expression or over-expression ofone or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased NUE, and an increasedwater use efficiency, in particular tolerance to drought conditions, ina plant upon expression or over-expression of endogenous and/orexogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, and anincreased water use efficiency, in particular tolerance to droughtconditions, in a plant upon expression or over-expression of one or moreendogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, and anincreased water use efficiency, in particular tolerance to droughtconditions, in a plant upon expression or over-expression of one or moreexogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased NUE, an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and an increased water use efficiency, in particular tolerance todrought conditions, in a plant upon expression or over-expression ofendogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and an increased water use efficiency, inparticular tolerance to drought conditions, in a plant upon expressionor over-expression of one or more endogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and an increased water use efficiency, inparticular tolerance to drought conditions, in a plant upon expressionor over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased nutrient efficiency,especially an increased NUE, and an increased yield in the absence ofstress as well as the absence of nutrient deficiencies, in a plant uponexpression or over-expression of endogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased nutrientefficiency, especially an increased NUE, and an increased yield in theabsence of stress as well as the absence of nutrient deficiencies, in aplant upon expression or over-expression of one or more endogenousgenes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased nutrientefficiency, especially an increased NUE, and an increased yield in theabsence of stress as well as the absence of nutrient deficiencies, in aplant upon expression or over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased nutrient efficiency,especially an increased NUE, an increased stress resistance,particularly abiotic stress resistance, especially an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and/or an increased water use efficiency, in particular tolerance todrought conditions, and an increased yield in the absence of stress aswell as the absence of nutrient deficiencies, in a plant upon expressionor over-expression of endogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased nutrientefficiency, especially an increased NUE, and an increased stressresistance, particularly abiotic stress resistance, especially anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and/or an increased water use efficiency, inparticular tolerance to drought conditions, and an increased yield inthe absence of stress as well as the absence of nutrient deficiencies,in a plant upon expression or over-expression of one or more endogenousgenes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased nutrientefficiency, especially an increased NUE, and an increased stressresistance, particularly abiotic stress resistance, especially anincreased low temperature tolerance, in particular an increasedtolerance to chilling, and/or an increased water use efficiency, inparticular tolerance to drought conditions, and an increased yield inthe absence of stress as well as the absence of nutrient deficiencies,in a plant upon expression or over-expression of one or more exogenousgenes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased NUE, an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and an increased yield in the absence of stress as well as the absenceof nutrient deficiencies, in a plant upon expression or over-expressionof endogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an NUE, an increased lowtemperature tolerance, in particular an increased tolerance to chilling,and an increased yield in the absence of stress as well as the absenceof nutrient deficiencies, in a plant upon expression or over-expressionof one or more endogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased low temperature tolerance, and an increased yield in theabsence of stress as well as the absence of nutrient deficiencies, in aplant upon expression or over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased NUE, an increased wateruse efficiency, in particular tolerance to drought conditions, and anincreased yield in the absence of stress as well as the absence ofnutrient deficiencies, in a plant upon expression or over-expression ofendogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased water use efficiency, in particular tolerance to droughtconditions, and an increased yield in the absence of stress as well asthe absence of nutrient deficiencies, in a plant upon expression orover-expression of one or more endogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased water use efficiency, in particular tolerance to droughtconditions, and an increased yield in the absence of stress as well asthe absence of nutrient deficiencies, in a plant upon expression orover-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of effecting an increased NUE, an increased lowtemperature tolerance, in particular an increased tolerance to chilling,an increased water use efficiency, in particular tolerance to droughtconditions, and an increased yield in the absence of stress as well asthe absence of nutrient deficiencies, in a plant upon expression orover-expression of endogenous and/or exogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased low temperature tolerance, in particular an increasedtolerance to chilling, an increased water use efficiency, in particulartolerance to drought conditions, and an increased yield in the absenceof stress as well as the absence of nutrient deficiencies, in a plantupon expression or over-expression of one or more endogenous genes.

In preferred embodiments thereof, this invention fulfills the need toidentify new, unique genes capable of effecting an increased NUE, anincreased low temperature tolerance, in particular an increasedtolerance to chilling, an increased water use efficiency, in particulartolerance to drought conditions, and an increased yield in the absenceof stress as well as the absence of nutrient deficiencies, in a plantupon expression or over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of conferring enhanced nutrient efficiency,especially enhanced NUE, to photosynthetic active organism, preferablyplants, upon expression or over-expression of one or more endogenousand/or exogenous genes.

In another embodiment thereof this invention fulfills the need toidentify new, unique genes capable of conferring enhanced nutrientefficiency, especially enhanced NUE, to photosynthetic active organism,preferably plants, upon expression or over-expression of one or moreendogenous genes.

In another embodiment thereof this invention fulfills the need toidentify new, unique genes capable of conferring enhanced nutrientefficiency, especially enhanced NUE, to photosynthetic active organism,preferably plants, upon expression or over-expression of one or moreexogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of conferring an increase of biomass production tophotosynthetic active organism, preferably plants, upon expression orover-expression of one or more endogenous and/or exogenous genes.

In another embodiment thereof this invention fulfills the need toidentify new, unique genes capable of conferring an increase of biomassproduction to photosynthetic active organism, preferably plants, uponexpression or over-expression of one or more endogenous genes.

In another embodiment thereof this invention fulfills the need toidentify new, unique genes capable of conferring an increase of biomassproduction to photosynthetic active organism, preferably plants, uponexpression or over-expression of one or more exogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of conferring an enhanced NUE in combination withan increase of biomass production to photosynthetic active organism,preferably plants, upon expression or over-expression of one or moreendogenous and/or exogenous genes.

In another embodiment thereof this invention fulfills the need toidentify new, unique genes capable of conferring an enhanced NUE incombination with an increase of biomass production to photosyntheticactive organism, preferably plants, upon expression or over-expressionof one or more endogenous genes.

In another embodiment this invention fulfills the need to identify new,unique genes capable of conferring an enhanced NUE in combination withan increase of biomass production to photosynthetic active organism,preferably plants, upon expression or over-expression of one or moreexogenous genes.

Thus, in the most preferred embodiments of the present invention, thisinvention fulfills the need to identify new, unique genes capable ofeffecting an increased nitrogen use efficiency (NUE), optionally anincreased low temperature tolerance, particularly chilling tolerance,optionally an increased water use efficiency, in particular tolerance todrought conditions, and optionally an increased yield in the absence ofstress as well as the absence of nutrient deficiencies. In each of theabove described preferred embodiments, it is preferred that said genesof the invention have the capacity of increasing or generating one ormore activities selected from the group consisting of2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydrolyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease. In these preferred embodimentsof the present invention, it is even more preferred that the increase orgeneration of one or more activities selected from the group consistingof 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease is effected by one or morenucleic acid sequences as shown in table I, column 5 or 7, by one ormore proteins encoded by one or more nucleic acid sequences as shown intable I, column 5 or 7, and/or by one or more protein(s) as depicted intable II, column 5 or 7. The need to identify such new, unique genes isparticularly fulfilled by providing the NUERP encoding genes disclosedherein.

Accordingly, the present invention relates to a method for producing atransgenic photosynthetic active organism or a part thereof, preferablya plant cell, a plant or a part thereof, resulting in increased yield,preferably with enhanced NUE and/or increased biomass production, ascompared to a corresponding non-transformed wild type photosyntheticactive organism or a part thereof, preferably a plant cell, a plant or apart thereof, which comprises

-   (a) increasing or generating one or more activities selected from    the group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease. in a photosynthetic    active organism or a part thereof, preferably a plant cell, a plant    or a part thereof, and-   (b) growing the photosynthetic active organism or a part thereof,    preferably a plant cell, a plant or a part thereof under conditions    which permit the development of a photosynthetic active organism or    a part thereof, preferably a plant cell, a plant or a part thereof,    showing increased yield, preferably enhanced NUE and/or increased    biomass production, as compared to a corresponding non-transformed    wild type photosynthetic active organism or a part thereof,    preferably a plant cell, a plant or a part thereof.

In an further embodiment, the present invention relates to a method forproducing a transgenic plant cell nucleus, a transgenic plant cell, atransgenic plant or a part thereof, resulting in increased yield ascompared to a corresponding non-transformed wild type plant cell, atransgenic plant or a part thereof, which comprises

(a) increasing or generating, in said plant cell nucleus, plant cell,plant or part thereof, one or more activities selected from the groupconsisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease;

-   (b) growing a plant cell, a plant or a part thereof under    conditions, preferably in presence or absence of nutrient deficiency    and/or abiotic stress, which permits the development of a plant    cell, a plant or a part thereof, showing increased yield as compared    to a corresponding non-transformed wild type plant cell, a    transgenic plant or a part thereto,    and-   (c) selecting the plant cell, a plant or a part thereof, showing    increased yield, preferably improved nutrient use efficiency and/or    abiotic stress resistance, as compared to a corresponding    non-transformed wild type plant cell, a transgenic plant or a part    thereof which shows visual symptoms of deficiency and/or death under    said conditions.

In an embodiment the present invention relates to a method for producinga transgenic photosynthetic active organism or a part thereof,preferably a plant cell, a plant or a part thereof with enhanced NUEand/or increased biomass production, as compared to a correspondingnon-transformed wild type photosynthetic active organism or a partthereof, preferably a plant cell, a plant or a part thereof, whichcomprises

-   (a) increasing or generating one or more activities selected from    the group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease. in a photosynthetic    active organism or a part thereof, preferably a plant cell, a plant    or a part thereof,-   (b) growing the photosynthetic active organism or a part thereof,    preferably a plant cell, a plant or a part thereof together with    non-transformed wildtype photosynthetic active organism or a part    thereof, preferably a plant, under conditions of limited nitrogen    supply,    and-   (c) selecting the photosynthetic active organism or a part thereof,    preferably a plant cell, a plant or a part thereof, with enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type photosynthetic active    organism or a part thereof, preferably a plant cell, a plant or a    part thereof, after the non-transformed wild type photosynthetic    active organism or a part thereof, preferably a plant cell, a plant    or a part thereof, show visual symptoms of deficiency and/or death.

In one embodiment the present invention relates to a method forproducing a transgenic photosynthetic active organism or a part thereof,preferably plant cell nucleus, a plant cell, a plant or a part thereof,resulting in increased yield, especially enhanced NUE and/or increasedbiomass production, as compared to a corresponding non-transformed wildtype photosynthetic active organism or a part thereof, preferably aplant cell, a plant or a part thereof, which comprises

-   (a) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3, preferably encoded by the    nucleic acid sequences as shown in table I, application no. 1,    column 5, in photosynthetic active organism or a part thereof,    preferably a plant cell nucleus, a plant cell, a plant or a part    thereof,    and-   (b) growing the photosynthetic active organism or a part thereof,    preferably a plant cell, a plant or a part thereof under conditions    which permit the development of a plant showing increased yield,    especially enhanced NUE and/or increased biomass production, as    compared to a corresponding non-transformed wild type photosynthetic    active organism or a part thereof, preferably a plant.

Accordingly, the present invention relates to a method for producing atransgenic plant cell, a plant or a part thereof, resulting in increasedyield, especially enhanced NUE and/or increased biomass production, ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof, which comprises

-   (a) increasing or generating one or more activities selected from    the group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease in an organelle,    especially the plastid, of a plant cell,    and-   (b) growing the plant cell under conditions which permit the    development of a plant showing increased yield, especially enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant.

In another embodiment the present invention relates to a method forproducing a transgenic plant cell, a plant or a part thereof, resultingin increased yield, especially enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof, which comprises

-   (a) increasing or generating one or more activities selected from    the group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease in the cytosol of a    plant cell,    and-   (b) growing the plant cell under conditions which permit the    development of a plant showing increased yield, especially enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant.

In one embodiment the present invention relates to a method forproducing a transgenic plant cell, a plant or a part thereof, resultingin increased yield, especially enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof, which comprises

-   (a) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3, preferably encoded by the    nucleic acid sequences as shown in table I, application no. 1,    column 5 or 7, in an organelle, especially in the plastid, of a    plant cell,    and-   (b) growing the plant cell under conditions which permit the    development of a plant showing increased yield, especially enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant.

In one embodiment the present invention relates to a method forproducing a transgenic plant cell, a plant or a part thereof, resultingin increased yield, especially enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof, which comprises

-   (a) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3, preferably encoded by the    nucleic acid sequences as shown in table I, application no. 1,    column 5 or 7, in the cytosol of a plant cell,    and-   (b) growing the plant cell under conditions which permit the    development of a plant showing increased yield, especially enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant.

In another embodiment the present invention is related to a method forproducing a transgenic plant cell, a plant or a part thereof, resultingin increased yield, especially enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof, which comprises

-   (a) increasing or generating one or more activities selected from    the group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, 60165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease. in an organelle of a    plant cell; or-   (b) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3 encoded by the nucleic acid    sequences as shown in table I, application no. 1, column 5 or 7,    which are joined to a nucleic acid sequence encoding a transit    peptide in a plant cell; or-   (c) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3 encoded by the nucleic acid    sequences as shown in table I, application no. 1, column 5 or 7,    which are joined to a nucleic acid sequence encoding an organelle    localization sequence, especially a chloroplast localization    sequence, in a plant cell,    and-   (d) growing the plant cell under conditions which permit the    development of a plant showing increased yield, especially enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant.

In another embodiment, the present invention relates to a method forproducing a transgenic plant cell, a plant or a part thereof, resultingin increased yield, especially enhanced nutrient efficiency, inparticular enhanced NUE and/or increased biomass production, andoptionally resulting in increased stress tolerance, especially abioticstress tolerance, preferably low temperature tolerance and/or increasedwater use efficiency, as compared to a corresponding non-transformedwild type plant cell, a plant or a part thereof, which comprises

-   (a) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3 encoded by the nucleic acid    sequences as shown in table I, application no. 1, column 5 or 7, in    an organelle of a plant through the transformation of the organelle,    or-   (b) increasing or generating the activity of a protein as shown in    table II, application no. 1, column 3 encoded by the nucleic acid    sequences as shown in table I, application no. 1, column 5 or 7 in    the plastid of a plant, or in one or more parts thereof through the    transformation of the plastids;    and-   (c) growing the plant cell under conditions which permit the    development of a plant showing increased yield, especially enhanced    nutrient efficiency, in particular enhanced NUE and/or increased    biomass production, and optionally resulting in increased stress    tolerance, especially abiotic stress tolerance, preferably low    temperature tolerance and/or increased water use efficiency, as    compared to a corresponding non-transformed wild type plant.

In principle the nucleic acid sequence encoding a transit peptide can beisolated from every organism such as microorganisms such as algae orplants containing plastids preferably chloroplasts. A “transit peptide”is an amino acid sequence, whose encoding nucleic acid sequence istranslated together with the corresponding structural gene. That meansthe transit peptide is an integral part of the translated protein andforms an amino terminal extension of the protein. Both are translated asso called “preprotein”. In general the transit peptide is cleaved offfrom the preprotein during or just after import of the protein into thecorrect cell organelle such as a plastid to yield the mature protein.The transit peptide ensures correct localization of the mature proteinby facilitating the transport of proteins through intracellularmembranes.

Preferred nucleic acid sequences encoding a transit peptide are derivedfrom a nucleic acid sequence encoding a protein finally resided in theplastid and stemming from an organism selected from the group consistingof the genera Acetabularia, Arabidopsis, Brassica, Capsicum,Chlamydomonas, Cururbita, Dunaliella, Euglena, Flayeria, Glycine,Helianthus, Hordeum, Lemna, Lolium, Lycopersion, Malus, Medicago,Mesembryanthemum, Nicotiana, Oenotherea, Oryza, Petunia, Phaseolus,Physcomitrella, Pinus, Pisum, Raphanus, Silene, Sinapis, Solanum,Spinacea, Stevia, Synechococcus, Triticum and Zea.

Advantageously such transit peptides, which are beneficially used in theinventive process, are derived from the nucleic acid sequence encoding aprotein selected from the group consisting of ribulose bisphosphatecarboxylase/oxygenase, 5-enolpyruvyl-shikimate-3-phosphate synthase,acetolactate synthase, chloroplast ribosomal protein CS17, Cs protein,ferredoxin, plastocyanin, ribulose bisphosphate carboxylase activase,tryptophan synthase, acyl carrier protein, plastid chaperonin-60,cytochrome c₅₅₂, 22-kDA heat shock protein, 33-kDa Oxygen-evolvingenhancer protein 1, ATP synthase γ subunit, ATP synthase δ subunit,chlorophyll-a/b-binding proteinII-1, Oxygen-evolving enhancer protein 2,Oxygen-evolving enhancer protein 3, photosystem I: P21, photosystem I:P28, photosystem I: P30, photosystem I: P35, photosystem I: P37,glycerol-3-phosphate acyltransferases, chlorophyll a/b binding protein,CAB2 protein, hydroxymethyl-bilane synthase, pyruvate-orthophosphatedikinase, CAB3 protein, plastid ferritin, ferritin, earlylight-inducible protein, glutamate-1-semialdehyde aminotransferase,protochlorophyllide reductase, starch-granule-bound amylase synthase,light-harvesting chlorophyll a/b-binding protein of photosystem II,major pollen allergen LoI p 5a, plastid ClpB ATP-dependent protease,superoxide dismutase, ferredoxin NADP oxidoreductase, 28-kDaribonucleoprotein, 31-kDa ribonucleoprotein, 33-kDa ribonucleoprotein,acetolactate synthase, ATP synthase CF₀ subunit 1, ATP synthase CF₀subunit 2, ATP synthase CF₀ subunit 3, ATP synthase CF₀ subunit 4,cytochrome f, ADP-glucose pyrophosphorylase, glutamine synthase,glutamine synthase 2, carbonic anhydrase, GapA protein,heat-shock-protein hsp21, phosphate translocator, plastid CIpAATP-dependent protease, plastid ribosomal protein CL24, plastidribosomal protein CL9, plastid ribosomal protein PsCL18, plastidribosomal protein PsCL25, DAHP synthase, starch phosphorylase, root acylcarrier protein II, betaine-aldehyde dehydrogenase, GapB protein,glutamine synthetase 2, phosphoribulokinase, nitrite reductase,ribosomal protein L12, ribosomal protein L13, ribosomal protein L21,ribosomal protein L35, ribosomal protein L40, triosephosphate-3-phosphoglyerate-phosphate translocator, ferredoxin-dependentglutamate synthase, glyceraldehyde-3-phosphate dehydrogenase,NADP-dependent malic enzyme and NADP-malate dehydrogenase.

More preferred the nucleic acid sequence encoding a transit peptide isderived from a nucleic acid sequence encoding a protein finally residedin the plastid and stemming from an organism selected from the groupconsisting of the species Acetabularia mediterranea, Arabidopsisthaliana, Brassica campestris, Brassica napus, Capsicum annuum,Chlamydomonas reinhardtii, Cururbita moschata, Dunaliella salina,Dunaliella tertiolecta, Euglena gracilis, Flayeria trinervia, Glycinemax, Helianthus annuus, Hordeum vulgare, Lemna gibba, Lolium perenne,Lycopersion esculentum, Malus domestica, Medicago falcata, Medicagosativa, Mesembryanthemum crystallinum, Nicotiana plumbaginifolia,Nicotiana sylvestris, Nicotiana tabacum, Oenotherea hookeri, Oryzasativa, Petunia hybrida, Phaseolus vulgaris, Physcomitrella patens,Pinus tunbergii, Pisum sativum, Raphanus sativus, Silene pratensis,Sinapis alba, Solanum tuberosum, Spinacea oleracea, Stevia rebaudiana,Synechococcus, Synechocystis, Triticum aestivum and Zea mays.

Even more preferred nucleic acid sequences are encoding transit peptidesas disclosed by von Heijne et al. (Plant Molecular Biology Reporter, 9(2), 104, (1991)), which are hereby incorparated by reference. Table Vshows some examples of the transit peptide sequences disclosed by vonHeijne et al. According to the disclosure of the invention especially inthe examples the skilled worker is able to link other nucleic acidsequences disclosed by von Heijne et al. to the nucleic acid sequencesshown in table I, application no. 1, columns 5 and 7. Most preferrednucleic acid sequences encoding transit peptides are derived from thegenus Spinacia such as chlorplast 30S ribosomal protein PSrp-1, rootacyl carrier protein II, acyl carrier protein, ATP synthase: γ subunit,ATP synthase: δ subunit, cytochrom f, ferredoxin I, ferredoxin NADPoxidoreductase (=FNR), nitrite reductase, phosphoribulokinase,plastocyanin or carbonic anhydrase. The skilled worker will recognizethat various other nucleic acid sequences encoding transit peptides caneasely isolated from plastid-localized proteins, which are expressedfrom nuclear genes as precursors and are then targeted to plastids. Suchtransit peptides encoding sequences can be used for the construction ofother expression constructs. The transit peptides advantageously used inthe inventive process and which are part of the inventive nucleic acidsequences and proteins are typically 20 to 120 amino acids, preferably25 to 110, 30 to 100 or 35 to 90 amino acids, more preferably 40 to 85amino acids and most preferably 45 to 80 amino acids in length andfunctions post-translationally to direct the protein to the plastidpreferably to the chloroplast. The nucleic acid sequences encoding suchtransit peptides are localized upstream of nucleic acid sequenceencoding the mature protein. For the correct molecular joining of thetransit peptide encoding nucleic acid and the nucleic acid encoding theprotein to be targeted it is sometimes necessary to introduce additionalbase pairs at the joining position, which forms restriction enzymerecognition sequences useful for the molecular joining of the differentnucleic acid molecules. This procedure might lead to very few additionalamino acids at the N-terminal of the mature imported protein, whichusually and preferably do not interfer with the protein function. In anycase, the additional base pairs at the joining position which formsrestriction enzyme recognition sequences have to be choosen with care,in order to avoid the formation of stop codons or codons which encodeamino acids with a strong influence on protein folding, like e.g.proline. It is preferred that such additional codons encode smallstructural flexible amino acids such as glycine or alanine.

As mentioned above the nucleic acid sequences coding for the proteins asshown in table II, application no. 1, column 3 and its homologs asdisclosed in table I, application no. 1, columns 5 and 7 can be joinedto a nucleic acid sequence encoding a transit peptide. This nucleic acidsequence encoding a transit peptide ensures transport of the protein tothe respective organelle, especially the plastid. The nucleic acidsequence of the gene to be expressed and the nucleic acid sequenceencoding the transit peptide are operably linked. Therefore the transitpeptide is fused in frame to the nucleic acid sequence coding forproteins as shown in table II, application no. 1, column 3 and itshomologs as disclosed in table I, application no. 1, columns 5 and 7.

The term “organelle” according to the invention shall mean for example“mitochondria” or preferably “plastid” (throughout the specification the“plural” shall comprise the “singular” and vice versa). The term“plastid” according to the invention is intended to include variousforms of plastids including proplastids, chloroplasts, chromoplasts,gerontoplasts, leucoplasts, amyloplasts, elaioplasts and etioplasts,preferably chloroplasts. They all have as a common ancestor theaforementioned proplasts.

Other transit peptides are disclosed by Schmidt et al. (J. Biol. Chem.268 (36), 27447 (1993)), Della-Cioppa et al. (Plant. Physiol. 84, 965(1987)), de Castro Silva Filho et al. (Plant Mol. Biol. 30, 769 (1996)),Zhao et al. (J. Biol. Chem. 270 (11), 6081 (1995)), Römer et al.(Biochem. Biophys. Res. Commun. 196 (3), 1414 (1993)), Keegstra et al.(Annu. Rev. Plant Physiol. Plant Mol. Biol. 40, 471 (1989)), Lubben etal. (Photosynthesis Res. 17, 173 (1988)) and Lawrence et al. (J. Biol.Chem. 272 (33), 20357 (1997)). A general review about targeting isdisclosed by Kermode Allison R. in Critical Reviews in Plant Science 15(4), 285 (1996) under the title “Mechanisms of Intracellular ProteinTransport and Targeting in Plant Cells.”

Favored transit peptide sequences, which are used in the inventiveprocess and which form part of the inventive nucleic acid sequences aregenerally enriched in hydroxylated amino acid residues (serine andthreonine), with these two residues generally constituting 20 to 35% ofthe total. They often have an amino-terminal region empty of Gly, Pro,and charged residues. Furthermore they have a number of smallhydrophobic amino acids such as valine and alanine and generally acidicamino acids are lacking. In addition they generally have a middle regionrich in Ser, Thr, Lys and Arg. Overall they have very often a netpositive charge.

Alternatively, nucleic acid sequences coding for the transit peptidesmay be chemically synthesized either in part or wholly according tostructure of transit peptide sequences disclosed in the prior art. Saidnatural or chemically synthesized sequences can be directly linked tothe sequences encoding the mature protein or via a linker nucleic acidsequence, which may be typically less than 500 base pairs, preferablyless than 450, 400, 350, 300, 250 or 200 base pairs, more preferablyless than 150, 100, 90, 80, 70, 60, 50, 40 or 30 base pairs and mostpreferably less than 25, 20, 15, 12, 9, 6 or 3 base pairs in length andare in frame to the coding sequence. Furthermore favorable nucleic acidsequences encoding transit peptides may comprise sequences derived frommore than one biological and/or chemical source and may include anucleic acid sequence derived from the amino-terminal region of themature protein, which in its native state is linked to the transitpeptide. In a preferred embodiment of the invention said amino-terminalregion of the mature protein is typically less than 150 amino acids,preferably less than 140, 130, 120, 110, 100 or 90 amino acids, morepreferably less than 80, 70, 60, 50, 40, 35, 30, 25 or 20 amino acidsand most preferably less than 19, 18, 17, 16, 15, 14, 13, 12, 11 or 10amino acids in length. But even shorter or longer stretches are alsopossible. In addition target sequences, which facilitate the transportof proteins to other cell compartments such as the vacuole, endoplasmicreticulum, golgi complex, glyoxysomes, peroxisomes or mitochondria maybe also part of the inventive nucleic acid sequence. The proteinstranslated from said inventive nucleic acid sequences are a kind offusion proteins that means the nucleic acid sequences encoding thetransit peptide for example the ones shown in table V, preferably thelast one of the table are joint to the nucleic acid sequences shown intable I, application no. 1, columns 5 and 7. The person skilled in theart is able to join said sequences in a functional manner.Advantageously the transit peptide part is cleaved off from the proteinpart shown in table II, application no. 1, columns 5 and 7 during thetransport preferably into the plastids. All products of the cleavage ofthe preferred transit peptide shown in the last line of table V havepreferably the N-terminal amino acid sequences QIA CSS or QIA EFQLTT infront of the start methionine of the protein mentioned in table II,application no. 1, columns 5 and 7. Other short amino acid sequences ofan range of 1 to 20 amino acids preferable 2 to 15 amino acids, morepreferable 3 to 10 amino acids most preferably 4 to 8 amino acids arealso possible in front of the start methionine of the protein motionedin table II, application no. 1, columns 5 and 7. In case of the aminoacid sequence QIA CSS the three amino acids in front of the startmethionine are stemming from the LIC (=ligatation independent cloning)cassette. Said short amino acid sequence is preferred in the case of theexpression of E. coli genes. In case of the amino acid sequence QIAEFQLTT the six amino acids in front of the start methionine are stemmingfrom the LIC cassette. Said short amino acid sequence is preferred inthe case of the expression of S. cerevisiae genes. The skilled workerknows that other short sequences are also useful in the expression ofthe genes mentioned in table I, application no. 1, columns 5 and 7.Furthermore the skilled worker is aware of the fact that there is not aneed for such short sequences in the expression of the genes.

TABLE V Examples of transit peptides disclosed by von Heijne et al. SEQTrans ID Pep Organism Transit Peptide NO: Reference  1 AcetabulariaMASIMMNKSVVLSKECAKPLATPK 17 Mol. Gen. mediterraneaVTLNKRGFATTIATKNREMMVWQP Genet. 218, FNNKMFETFSFLPP 445 (1989)  2Arabidopsis MAASLQSTATFLQSAKIATAPSRG 18 EMBO J. 8, thalianaSSHLRSTQAVGKSFGLETSSARLT 3187 (1989) CSFQSDFKDFTGKCSDAVKIAGFALATSALVVSGASAEGAPK  3 Arabidopsis MAQVSRICNGVQNPSLICNLSKSS 19 Mol. Gen.thaliana QRKSPLSVSLKTQQHPRAYPISSS Genet. 210, WGLKKSGMTLIGSELRPLKVMSSV437 (1987) STAEKASEIVLQPIREISGLIKLP  4 ArabidopsisMAAATTTTTTSSSISFSTKPSPSS 20 Plant Phys- thalianaSKSPLPISRFSLPFSLNPNKSSSS iol. 85, 1110 SRRRGIKSSSPSSISAVLNTTTNV (1987)TTTPSPTKPTKPETFISRFAPDQP RKGA  5 Arabidopsis MITSSLTCSLQALKLSSPFAHGST 21J. Biol. thaliana PLSSLSKPNSFPNHRMPALVPV Chem. 265, 2763 (1990)  6Arabidopsis MASLLGTSSSAIWASPSLSSPSSKP 22 EMBO J. 9, thalianaSSSPICFRPGKLFGSKLNAGIQI 1337 (1990) RPKKNRSRYHVSVMNVATEINSTEQVVGKFDSKKSARPVYPFAAI  7 Arabidopsis MASTALSSAIVGTSFIRRSPAPISL 23Plant Phys- thaliana RSLPSANTQSLFGLKSGTARGG iol. 93, 572 RVVAM (1990)  8Arabidopsis MAASTMALSSPAFAGKAVNLSPAA 24 Nucl. Acids thalianaSEVLGSGRVTNRKTV Res. 14, 4051 (1986)  9 ArabidopsisMAAITSATVTIPSFTGLKLAVSSK 25 Gene 65, 59 thalianaPKTLSTISRSSSATRAPPKLALKS (1988) SLKDFGVIAVATAASIVLAGNAMAMEVLLGSDDGSLAFVPSEFT 10 Arabidopsis MAAAVSTVGAINRAPLSLNGSGSG 26Nucl. Acids thaliana AVSAPASTFLGKKVVTVSRFAQSN Res. 17,KKSNGSFKVLAVKEDKQTDGDRWR 2871 (1989) GLAYDTSDDQIDI 11 ArabidopsisMKSSMLSSTAWTSPAQATMVAPF 27 Plant Mol. thaliana TGLKSSASFPVTRKANNDITSITSBiol. 11, 745 NGGRVSC (1988) 12 Arabidopsis MAASGTSATFRASVSSAPSSSSQL 28Proc. Natl. thaliana THLKSPFKAVKYTPLPSSRSKSSS Acad. Sci.FSVSCTIAKDPPVLMAAGSDPALW USA, 86, QRPDSFGRFGKFGGKYVPE 4604 (1989) 13Brassica MSTTFCSSVCMQATSLAATTRISF 29 Nucl. Acids campestrisQKPALVSTTNLSFNLRRSIPTRFS Res. 15, ISCAAKPETVEKVSKIVKKQLSLK 7197 (1987)DDQKVVAE 14 Brassica MATTFSASVSMQATSLATTTRISF 30 Eur. J. Bio- napusQKPVLVSNHGRTNLSFNLSRTRLSI chem. 174, SC 287 (1988) 15 Chlamydo-MQALSSRVNIAAKPQRAQRLWRA 31 Plant Mol. monas EEVKAAPKKEVGPKRGSLVKBiol. 12, 463 reinhardtii (1989) 16 Cucurbita MAELIQDKESAQSAATAAAASSGY32 FEBS Lett. moschata ERRNEPAHSRK- 238, 424 FLEVRSEEELLSCIKK (1988) 17Spinacea MSTINGCLTSISPSRTQLKNTSTL 33 J. Biol. oleraceaRPTFIANSRVNPSSSVPPSLIRNQ Chem. 265, PVFAAPAPIITPTL (10) 5414 (1990) 18Spinacea MTTAVTAAVSFPSTKTTSLSARCS 34 Curr. Genet. oleraceaSVISPDKISYKKVPLYYRNVSATG 13, 517 KMGPIRAQIASDVEAPPPAPAK- (1988) VEKMS 19Spinacea MTTAVTAAVSFPSTKTTSLSARSS 35 oleracea SVISPDKISYKKVPLYYRNVSATGKMGPIRA

Alternatively to the targeting of the sequences shown in table II,application no. 1, columns 5 and 7, preferably of sequences in generalencoded in the nucleus with the aid of the targeting sequences mentionedfor example in table V alone or in combination with other targetingsequences preferably into the plastids, the nucleic acids of theinvention can directly be introduced into the plastidal genome.Therefore in a preferred embodiment the nucleic acid sequences shown intable I, application no. 1, columns 5 and 7 are directly introduced andexpressed in plastids.

The term “introduced” in the context of this specification shall meanthe insertion of a nucleic acid sequence into the organism by means of a“transfection”, “transduction” or preferably by “transformation”.

A plastid, such as a chloroplast, has been “transformed” by an exogenous(preferably foreign) nucleic acid sequence if nucleic acid sequence hasbeen introduced into the plastid that means that this sequence hascrossed the membrane or the membranes of the plastid. The foreign DNAmay be integrated (covalently linked) into plastid DNA making up thegenome of the plastid, or it may remain unintegrated (e.g., by includinga chloroplast origin of replication). “Stably” integrated DNA sequencesare those, which are inherited through plastid replication, therebytransferring new plastids, with the features of the integrated DNAsequence to the progeny.

For expression a person skilled in the art is familiar with differentmethods to introduce the nucleic acid sequences into differentorganelles such as the preferred plastids. Such methods are for exampledisclosed by Maiga P. (Annu. Rev. Plant Biol. 55, 289 (2004)), Evans T.(WO 2004/040973), McBride K.E. et al. (U.S. Pat. No. 5,455,818), DaniellH. et al. (U.S. Pat. No. 5,932,479 and U.S. Pat. No. 5,693,507) andStraub J. M. et al. (U.S. Pat. No. 6,781,033). A preferred method is thetransformation of microspore-derived hypocotyl or cotyledonary tissue(which are green and thus contain numerous plastids) leaf tissue andafterwards the regeneration of shoots from said transformed plantmaterial on selective medium. As methods for the transformationbombarding of the plant material or the use of independently replicatingshuttle vectors are well known by the skilled worker. But also aPEG-mediated transformation of the plastids or Agrobacteriumtransformation with binary vectors is possible. Useful markers for thetransformation of plastids are positive selection markers for examplethe chloramphenicol-, streptomycin-, kanamycin-, neomycin-, amikamycin-,spectinomycin-, triazine- and/or lincomycin-resistance genes. Asadditional markers named in the literature often as secondary markers,genes coding for the resistance against herbicides such asphosphinothricin (=glufosinate, BASTA™, Liberty™, encoded by the bargene), glyphosate (=N(phosphonomethyl)glycine, Roundup™, encoded by the5-enolpyruvylshikimate-3-phosphate synthase gene=epsps), sulfonylureas(like Staple™, encoded by the acetolactate synthase (ALS) gene),imidazolinones [=IMI, like imazethapyr, imazamox, Clearfield™, encodedby the acetohydroxyacid synthase (AHAS) gene, also known as acetolactatesynthase (ALS) gene] or bromoxynil (=Buctril™, encoded by the oxy gene)or genes coding for antibiotics such as hygromycin or G418 are usefulfor further selection. Such secondary markers are useful in the casewhen most genome copies are transformed. In addition negative selectionmarkers such as the bacterial cytosine deaminase (encoded by the codAgene) are also useful for the transformation of plastids.

To increase the possibility of identification of transformants it isalso desirable to use reporter genes other then the aforementionedresistance genes or in addition to said genes. Reporter genes are forexample β-galactosidase-, β-glucuronidase-(GUS), alkaline phosphatase-and/or green-fluorescent protein-genes (GFP).

For the inventive process it is of great advantage that by transformingthe plastids the intraspecies specific transgene flow is blocked,because a lot of species such as corn, cotton and rice have a strictmaternal inheritance of plastids. By placing the genes specified intable I, application no. 1, columns 5 and 7 or active fragments thereofin the plastids of plants, these genes will not be present in the pollenof said plants.

A further preferred embodiment of the invention relates to the use of socalled “chloroplast localization sequences”, in which a first RNAsequence or molecule is capable of transporting or “chaperoning” asecond RNA sequence, such as a RNA sequence transcribed from thesequences depicted in table I, application no. 1, columns 5 and 7 or asequence encoding a protein, as depicted in table II, application no. 1,columns 5 and 7, from an external environment inside a cell or outside aplastid into a chloroplast. In one embodiment the chloroplastlocalization signal is substantially similar or complementary to acomplete or intact viroid sequence. The chloroplast localization signalmay be encoded by a DNA sequence, which is transcribed into thechloroplast localization RNA. The term “viroid” refers to a naturallyoccurring single stranded RNA molecule (Flores, C. R. Acad Sci III. 324(10), 943 (2001)). Viroids usually contain about 200-500 nucleotides andgenerally exist as circular molecules. Examples of viroids that containchloroplast localization signals include but are not limited to ASBVd,PLMVd, CChMVd and ELVd. The viroid sequence or a functional part of itcan be fused to the sequences depicted in table I, application no. 1,columns 5 and 7 or a sequence encoding a protein, as depicted in tableII, application no. 1, columns 5 and 7 in such a manner that the viroidsequence transports a sequence transcribed from a sequence as depictedin table I, application no. 1, columns 5 and 7 or a sequence encoding aprotein as depicted in table II, application no. 1, columns 5 and 7 intothe chloroplasts. A preferred embodiment uses a modified ASBVd (Navarroet al., Virology. 268 (1), 218 (2000)).

In a further specific embodiment the protein to be expressed in theplastids such as the proteins depicted in table II, application no. 1,columns 5 and 7 are encoded by different nucleic acids. Such a method isdisclosed in WO 2004/040973, which shall be incorporated by reference.WO 2004/040973 teaches a method, which relates to the translocation ofan RNA corresponding to a gene or gene fragment into the chloroplast bymeans of a chloroplast localization sequence. The genes, which should beexpressed in the plant or plants cells, are split into nucleic acidfragments, which are introduced into different compartments in the plante.g. the nucleus, the plastids and/or mitochondria. Additionally plantcells are described in which the chloroplast contains a ribozyme fusedat one end to an RNA encoding a fragment of a protein used in theinventive process such that the ribozyme can trans-splice thetranslocated fusion RNA to the RNA encoding the gene fragment to formand as the case may be reunite the nucleic acid fragments to an intactmRNA encoding a functional protein for example as disclosed in table II,columns 5 and 7.

In a preferred embodiment of the invention the nucleic acid sequences asshown in table I, application no. 1, columns 5 and 7 used in theinventive process are transformed into plastids, which are metabolicallyactive. Those plastids should preferably maintain at a high copy numberin the plant or plant tissue of interest, most preferably thechloroplasts found in green plant tissues, such as leaves or cotyledonsor in seeds.

For a good expression in the plastids the nucleic acid sequences asshown in table I, application no. 1, columns 5 and 7 are introduced intoan expression cassette using a preferably a promoter and terminator,which are active in plastids preferably a chloroplast promoter. Examplesof such promoters include the psbA promoter from the gene from spinachor pea, the rbcL promoter, and the atpB promoter from corn.

For the purposes of the description of the present invention, the terms“cytoplasmic” shall indicate, that the nucleic acid of the invention isexpressed without the addition of an non-natural transit peptideencoding sequence. A non-natural transit peptide encoding sequence is asequence which is not a natural part of a nucleic acid of the invention,e.g. of the nucleic acids depicted in table I column 5 or 7, but israther added by molecular manipulation steps as for example described inthe example under “plastid targeted expression”. Therfore the terms“cytoplasmic” shall not exclude a targeted localisation to any cellcompartment for the products of the inventive nucleic acid sequences bytheir naturally occurring sequence properties within the background ofthe transgenic organism. The subcellular location of the maturepolypetide derived from the enclosed sequences can be predicted by askilled person for the organism (plant) by using software tools likeTargetP (Emanuelsson et al., (2000), Predicting subcellular localizationof proteins based on their N-terminal amino acid sequence., J. Mol.Biol. 300, 1005-1016.), ChloroP (Emanuelsson et al. (1999), ChloroP, aneural network-based method for predicting chloroplast transit peptidesand their cleavage sites., Protein Science, 8: 978-984.) or otherpredictive software tools (Emanuelsson et al. (2007), Locating proteinsin the cell using TargetP, SignalP, and related tools., Nature Protocols2, 953-971).

Comprises/comprising and grammatical variations thereof when used inthis specification are to be taken to specify the presence of statedfeatures, integers, steps or components or groups thereof, but not topreclude the presence or addition of one or more other features,integers, steps, components or groups thereof.

In accordance with the invention, the term “plant cell” or the term“organism” as understood herein relates always to a plant cell or anorganelle thereof, preferably a plastid, more preferably chloroplast.

As used herein, “plant” is meant to include not only a whole plant butalso a part thereof i.e., one or more cells, and tissues, including forexample, leaves, stems, shoots, roots, flowers, fruits and seeds.

Surprisingly it was found, that the transgenic expression of a proteinas shown in table II, application no. 1, column 3, especially from theSaccaromyces cerevisiae and/or the transgenic expression of a protein asshown in table II, application no. 1, column 3, especially from the E.coli, in a plant, such as Arabidopsis thaliana for example, conferred ayield increase, especially an enhanced NUE and/or increased biomassproduction, to the transgenic plant cell, plant or a part thereof ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof. In addition the yield increase may be generatedby an increased tolerance to stress, especially abiotic stress,particularly low temperature stress and/or enhanced water use efficiencyand/or enhanced intrinsic yield in the absence of nutrient deficienciesas well as stress conditions.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 38, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 38 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 38 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 38 by exchanging the stop codon taaby tga) or a polypeptide SEQ ID NO. 39, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 38 or polypeptide SEQ ID NO. 39, respectively,is increased or generated, or if the activity “b0017-protein” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 42, or the activity of a polypeptide encoded bya nucleic acid molecule comprising the nucleic acid SEQ ID NO. 42 or apolypeptide SEQ ID NO. 43, respectively, is increased or generated, e.g.if the activity of such a nucleic acid molecule or a polypeptidecomprising the nucleic acid or polypeptide or the consensus sequence orthe polypeptide motif, as depicted in table I, II or IV, application no.1, column 7 in the respective same line as the nucleic acid molecule SEQID NO. 42 or polypeptide SEQ ID NO. 43, respectively, is increased orgenerated, or if the activity “transport protein” is increased orgenerated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.15-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 123, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 123 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 123 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 123 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 124, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 123 or polypeptide SEQ ID NO. 124,respectively, is increased or generated, or if the activity“hydroxymyristol acyl carrier protein dehydratase” is increased orgenerated in an plant cell, plant or part thereof, especially withplastidic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.41-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.33-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli K12 nucleicacid molecule SEQ ID NO. 380, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 380 ora polypeptide SEQ ID NO. 381, respectively, is increased or generated,e.g. if the activity of such a nucleic acid molecule or a polypeptidecomprising the nucleic acid or polypeptide or the consensus sequence orthe polypeptide motif, as depicted in table I, II or IV, application no.1, column 7 in the respective same line as the nucleic acid molecule SEQID NO. 380 or polypeptide SEQ ID NO. 381, respectively, is increased orgenerated, or if the activity “gamma-glutamyl kinase” is increased orgenerated in an plant cell, plant or part thereof, especially withplastidic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.16-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 679, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 679 ora polypeptide SEQ ID NO. 680, respectively, is increased or generated,e.g. if the activity of such a nucleic acid molecule or a polypeptidecomprising the nucleic acid or polypeptide or the consensus sequence orthe polypeptide motif, as depicted in table I, II or IV, application no.1, column 7 in the respective same line as the nucleic acid molecule SEQID NO. 679 or polypeptide SEQ ID NO. 680, respectively, is increased orgenerated, or if the activity “alpha-glucosidase” is increased orgenerated in an plant cell, plant or part thereof, especially withplastidic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.10-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 812, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 812 ora polypeptide SEQ ID NO. 813, respectively, is increased or generated,e.g. if the activity of such a nucleic acid molecule or a polypeptidecomprising the nucleic acid or polypeptide or the consensus sequence orthe polypeptide motif, as depicted in table I, II or IV, application no.1, column 7 in the respective same line as the nucleic acid molecule SEQID NO. 812 or polypeptide SEQ ID NO. 813, respectively, is increased orgenerated, or if the activity “adenylate kinase” is increased orgenerated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.09-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 1055, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 1055or a polypeptide SEQ ID NO. 1056, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 1055 or polypeptide SEQ ID NO. 1056,respectively, is increased or generated, or if the activity“2-dehydro-3-deoxy-phosphoheptonate aldolase” is increased or generatedin an plant cell, plant or part thereof, especially with plastidiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.15-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.23-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 1563, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 1563or a polypeptide SEQ ID NO. 1564, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 1563 or polypeptide SEQ ID NO. 1564,respectively, is increased or generated, or if the activity“molybdopterin biosynthesis protein” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.20-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 1705, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 1705or a polypeptide SEQ ID NO. 1706, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 1705 or polypeptide SEQ ID NO. 1706,respectively, is increased or generated, or if the activity“hydroxylamine reductase” is increased or generated in an plant cell,plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.17-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 1844, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 1844or a polypeptide SEQ ID NO. 1845, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 1844 or polypeptide SEQ ID NO. 1845,respectively, is increased or generated, or if the activity “prolinedehydrogenase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 1950, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 1950or a polypeptide SEQ ID NO. 1951, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 1950 or polypeptide SEQ ID NO. 1951,respectively, is increased or generated, or if the activity “PhoH-likeprotein” is increased or generated in an plant cell, plant or partthereof, especially with plastidic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.10-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.17-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 1975, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 1975or a polypeptide SEQ ID NO. 1976, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 1975 or polypeptide SEQ ID NO. 1976,respectively, is increased or generated, or if the activity “isomerase”is increased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.18-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2127, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 2127 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 2127 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 2127 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 2128, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2127 or polypeptide SEQ ID NO. 2128,respectively, is increased or generated, or if the activity“b1933-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.55-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.12-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2135, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 2135 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 2135 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 2135 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 2136, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2135 or polypeptide SEQ ID NO. 2136,respectively, is increased or generated, or if the activity“glycosyltransferase” is increased or generated in an plant cell, plantor part thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.14-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli K12 nucleicacid molecule SEQ ID NO. 2171, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 2171or a polypeptide SEQ ID NO. 2172, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2171 or polypeptide SEQ ID NO. 2172,respectively, is increased or generated, or if the activity“b2165-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.24-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli K12 nucleicacid molecule SEQ ID NO. 2297, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 2297 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 2297 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 2297 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 2298, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2297 or polypeptide SEQ ID NO. 2298,respectively, is increased or generated, or if the activity “short chainfatty acid transporter” is increased or generated in an plant cell,plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.36-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2426, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 2426 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 2426 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 2426 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 2427, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2426 or polypeptide SEQ ID NO. 2427,respectively, is increased or generated, or if the activity“b2238-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance, especiallyan increased tolerance to low temperatures, and/or an increased yield,in the absence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.26-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.19-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.18-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2426, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 2426 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 2426 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 2426 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 2427, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2426 or polypeptide SEQ ID NO. 2427,respectively, is increased or generated, or if the activity“b2238-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance, especiallyan increased tolerance to drought conditions, and/or an increased yield,in the absence of a nutrient deficiency as well as stress conditions.

Particularly, an increase from 1.05-fold to 1.11-fold plus at least 100%thereof under drought conditions is conferred; also particularly, ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli K12 nucleicacid molecule SEQ ID NO. 2452, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 2452 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 2452 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 2452 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 2453, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2452 or polypeptide SEQ ID NO. 2453,respectively, is increased or generated, or if the activity“lysine/arginine/ornithine transporter subunit” is increased orgenerated in an plant cell, plant or part thereof, especially withplastidic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.18-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.25-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.20-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2551, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 2551or a polypeptide SEQ ID NO. 2552, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2551 or polypeptide SEQ ID NO. 2552,respectively, is increased or generated, or if the activity“b2431-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.47-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.34-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.17-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli K12 nucleicacid molecule SEQ ID NO. 2600, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 2600or a polypeptide SEQ ID NO. 2601, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2600 or polypeptide SEQ ID NO. 2601,respectively, is increased or generated, or if the activity “chorismatemutase T/prephenate dehydrogenase (bifunctional)” is increased orgenerated in an plant cell, plant or part thereof, especially withplastidic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.12-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.16-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2668, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 2668or a polypeptide SEQ ID NO. 2669, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2668 or polypeptide SEQ ID NO. 2669,respectively, is increased or generated, or if the activity“b2766-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.10-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.26-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.20-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 2772, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 2772or a polypeptide SEQ ID NO. 2773, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2772 or polypeptide SEQ ID NO. 2773,respectively, is increased or generated, or if the activity “glycinedecarboxylase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.65-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 3117, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 3117or a polypeptide SEQ ID NO. 3118, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3117 or polypeptide SEQ ID NO. 3118,respectively, is increased or generated, or if the activity “threonineammonia-lyase” is increased or generated in an plant cell, plant or partthereof, especially with plastidic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.16-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 3390, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 3390 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 3390 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 3390 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 3391, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3390 or polypeptide SEQ ID NO. 3391,respectively, is increased or generated, or if the activity“b3120-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.28-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.15-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.39-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 3396, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 3396or a polypeptide SEQ ID NO. 3397, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3396 or polypeptide SEQ ID NO. 3397,respectively, is increased or generated, or if the activity “outermembrane usher protein” is increased or generated in an plant cell,plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli K12 nucleicacid molecule SEQ ID NO. 3470, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 3470or a polypeptide SEQ ID NO. 3471, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3470 or polypeptide SEQ ID NO. 3471,respectively, is increased or generated, or if the activity“glycerol-3-phosphate transporter subunit” is increased or generated inan plant cell, plant or part thereof, especially with plastidiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.10-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.23-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 3563, or a nucleic acid which differs fromnucleic acid SEQ ID NO. 3563 by exchanging the stop codon taa by tga, orthe activity of a polypeptide encoded by a nucleic acid moleculecomprising the nucleic acid SEQ ID NO. 3563 (or a nucleic acid whichdiffers from nucleic acid SEQ ID NO. 3563 by exchanging the stop codontaa by tga) or a polypeptide SEQ ID NO. 3564, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3563 or polypeptide SEQ ID NO. 3564,respectively, is increased or generated, or if the activity“hydro-lyase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 3770, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 3770or a polypeptide SEQ ID NO. 3771, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3770 or polypeptide SEQ ID NO. 3771,respectively, is increased or generated, or if the activity“lysophospholipase” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 3868, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 3868 or a polypeptide SEQ ID NO. 3869, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3868 or polypeptide SEQ ID NO. 3869,respectively, is increased or generated, or if the activity“yal019w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.14-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 3895, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 3895 or a polypeptide SEQ ID NO. 3896, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3895 or polypeptide SEQ ID NO. 3896,respectively, is increased or generated, or if the activity “carnitineacetyltransferase” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.38-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.43-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 3953, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 3953 or a polypeptide SEQ ID NO. 3954, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3953 or polypeptide SEQ ID NO. 3954,respectively, is increased or generated, or if the activity“Transcriptional activator” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.15-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4111, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4111 or a polypeptide SEQ ID NO. 4112, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4111 or polypeptide SEQ ID NO. 4112,respectively, is increased or generated, or if the activity “splicingfactor” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.10-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4149, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4149 or a polypeptide SEQ ID NO. 4150, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4149 or polypeptide SEQ ID NO. 4150,respectively, is increased or generated, or if the activity“autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4162, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4162 or a polypeptide SEQ ID NO. 4163, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4162 or polypeptide SEQ ID NO. 4163,respectively, is increased or generated, or if the activity “microsomalbeta-keto-reductase” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.07-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4235, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4235 or a polypeptide SEQ ID NO. 4236, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4235 or polypeptide SEQ ID NO. 4236,respectively, is increased or generated, or if the activity“UDP-N-acetyl-glucosamine-1-P transferase” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.16-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4235, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4235 or a polypeptide SEQ ID NO. 4236, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4235 or polypeptide SEQ ID NO. 4236,respectively, is increased or generated, or if the activity“UDP-N-acetyl-glucosamine-1-P transferase” is increased or generated inan plant cell, plant or part thereof, especially with plastidiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions.

Particularly, an increase from 1.05-fold to 1.26-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.29-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4280, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4280 or a polypeptide SEQ ID NO. 4281, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4280 or polypeptide SEQ ID NO. 4281,respectively, is increased or generated, or if the activity“ybr262c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.31-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4288, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4288 or a polypeptide SEQ ID NO. 4289, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4288 or polypeptide SEQ ID NO. 4289,respectively, is increased or generated, or if the activity “proteinnecessary for structural stability of L-A double-stranded RNA-containingparticles” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.31-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.24-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4315, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4315 or a polypeptide SEQ ID NO. 4316, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4315 or polypeptide SEQ ID NO. 4316,respectively, is increased or generated, or if the activity“YDR070C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.20-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.47-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4325, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4325 or a polypeptide SEQ ID NO. 4326, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4325 or polypeptide SEQ ID NO. 4326,respectively, is increased or generated, or if the activity “chaperone”is increased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.29-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.09-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4335, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4335 or a polypeptide SEQ ID NO. 4336, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4335 or polypeptide SEQ ID NO. 4336,respectively, is increased or generated, or if the activity“helix-loop-helix transcription activator that bindsinositol/choline-responsive elements” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4346, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4346 or a polypeptide SEQ ID NO. 4347, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4346 or polypeptide SEQ ID NO. 4347,respectively, is increased or generated, or if the activity “golgimembrane exchange factor subunit” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.22-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.14-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4361, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4361 or a polypeptide SEQ ID NO. 4362, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4361 or polypeptide SEQ ID NO. 4362,respectively, is increased or generated, or if the activity“dihydrosphingosine phosphate lyase” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.13-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4361, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4361 or a polypeptide SEQ ID NO. 4362, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4361 or polypeptide SEQ ID NO. 4362,respectively, is increased or generated, or if the activity“dihydrosphingosine phosphate lyase” is increased or generated in anplant cell, plant or part thereof, especially with plastidiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions.

Particularly, an increase from 1.05-fold to 1.35-fold plus at least 100%thereof under drought conditions is conferred as compared to acorresponding non-transformed wild type plant cell, a plant or a partthereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4402, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4402 or a polypeptide SEQ ID NO. 4403, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4402 or polypeptide SEQ ID NO. 4403,respectively, is increased or generated, or if the activity “ubiquitinregulatory protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.38-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.24-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.14-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4431, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4431 or a polypeptide SEQ ID NO. 4432, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4431 or polypeptide SEQ ID NO. 4432,respectively, is increased or generated, or if the activity“ydr355c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.34-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4435, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4435 or a polypeptide SEQ ID NO. 4436, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4435 or polypeptide SEQ ID NO. 4436,respectively, is increased or generated, or if the activity“lysine-specific metalloprotease” is increased or generated in an plantcell, plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.16-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.10-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.61-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4485, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4485 or a polypeptide SEQ ID NO. 4486, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4485 or polypeptide SEQ ID NO. 4486,respectively, is increased or generated, or if the activity “subunit ofthe transport protein particle (TRAPP) complex of the cis-Golgi” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction. Particularly, an increase from 1.1-fold to 1.20-fold plus atleast 100% thereof under conditions of nitrogen deficiency is conferredas compared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4506, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4506 or a polypeptide SEQ ID NO. 4507, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4506 or polypeptide SEQ ID NO. 4507,respectively, is increased or generated, or if the activity“myo-inositol transporter” is increased or generated in an plant cell,plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.16-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.23-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.10-fold plus at least 100% thereof under droughtconditions; also particularly, an increase from 1.05-fold to 1.14-foldplus at least 100% thereof of yield in the absence of nutrientdeficiency as well as stress conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4790, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4790 or a polypeptide SEQ ID NO. 4791, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4790 or polypeptide SEQ ID NO. 4791,respectively, is increased or generated, or if the activity “SM complexB protein for mRNA splicing” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.13-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.10-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4806, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4806 or a polypeptide SEQ ID NO. 4807, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4806 or polypeptide SEQ ID NO. 4807,respectively, is increased or generated, or if the activity“YFR007W-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.36-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 4836, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 4836 or a polypeptide SEQ ID NO. 4837, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 4836 or polypeptide SEQ ID NO. 4837,respectively, is increased or generated, or if the activity“oxidoreductase” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.22-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.32-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5311, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5311 or a polypeptide SEQ ID NO. 5312, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5311 or polypeptide SEQ ID NO. 5312,respectively, is increased or generated, or if the activity“transcription elongation factor” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.26-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5346, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5346 or a polypeptide SEQ ID NO. 5347, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5346 or polypeptide SEQ ID NO. 5347,respectively, is increased or generated, or if the activity “cytosoliccatalase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.13-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5533, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5533 or a polypeptide SEQ ID NO. 5534, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5533 or polypeptide SEQ ID NO. 5534,respectively, is increased or generated, or if the activity“ygr122c-a-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.30-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5551, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5551 or a polypeptide SEQ ID NO. 5552, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5551 or polypeptide SEQ ID NO. 5552,respectively, is increased or generated, or if the activity “v-SNAREbinding protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5559, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5559 or a polypeptide SEQ ID NO. 5560, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5559 or polypeptide SEQ ID NO. 5560,respectively, is increased or generated, or if the activity “proteininvolved in sphingolipid biosynthesis” is increased or generated in anplant cell, plant or part thereof, especially with Cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5602, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5602 or a polypeptide SEQ ID NO. 5603, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5602 or polypeptide SEQ ID NO. 5603,respectively, is increased or generated, or if the activity“mitochondrial ribosomal protein of the small subunit” is increased orgenerated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5608, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5608 or a polypeptide SEQ ID NO. 5609, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5608 or polypeptide SEQ ID NO. 5609,respectively, is increased or generated, or if the activity“phosphatidylserine decarboxylase” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.12-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5614, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5614 or a polypeptide SEQ ID NO. 5615, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5614 or polypeptide SEQ ID NO. 5615,respectively, is increased or generated, or if the activity“cholinephosphate cytidylyltransferase” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.55-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5666, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5666 or a polypeptide SEQ ID NO. 5667, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5666 or polypeptide SEQ ID NO. 5667,respectively, is increased or generated, or if the activity“ygr266w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.34-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5701, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5701 or a polypeptide SEQ ID NO. 5702, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5701 or polypeptide SEQ ID NO. 5702,respectively, is increased or generated, or if the activity “cell wallendo-beta-1,3-glucanase” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5750, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5750 or a polypeptide SEQ ID NO. 5751, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5750 or polypeptide SEQ ID NO. 5751,respectively, is increased or generated, or if the activity“ygr290w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5754, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5754 or a polypeptide SEQ ID NO. 5755, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5754 or polypeptide SEQ ID NO. 5755,respectively, is increased or generated, or if the activity“yhl021c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.12-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5778, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5778 or a polypeptide SEQ ID NO. 5779, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5778 or polypeptide SEQ ID NO. 5779,respectively, is increased or generated, or if the activity “v-SNAREprotein involved in Golgi transport” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5812, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5812 or a polypeptide SEQ ID NO. 5813, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5812 or polypeptide SEQ ID NO. 5813,respectively, is increased or generated, or if the activity“mitochondrial seryl-tRNA synthetase” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5967, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5967 or a polypeptide SEQ ID NO. 5968, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5967 or polypeptide SEQ ID NO. 5968,respectively, is increased or generated, or if the activity“yhr127w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.36-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5973, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5973 or a polypeptide SEQ ID NO. 5974, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5973 or polypeptide SEQ ID NO. 5974,respectively, is increased or generated, or if the activity “aromaticamino acid aminotransferase II” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.39-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 5973, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 5973 or a polypeptide SEQ ID NO. 5974, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 5973 or polypeptide SEQ ID NO. 5974,respectively, is increased or generated, or if the activity “aromaticamino acid aminotransferase II” is increased or generated in an plantcell, plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.05-fold to 1.13-fold plus at least 100%thereof under low temperature conditions is conferred as compared to acorresponding non-transformed wild type plant cell, a plant or a partthereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6027, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6027 or a polypeptide SEQ ID NO. 6028, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6027 or polypeptide SEQ ID NO. 6028,respectively, is increased or generated, or if the activity“glucoamylase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 3.09-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6027, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6027 or a polypeptide SEQ ID NO. 6028, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6027 or polypeptide SEQ ID NO. 6028,respectively, is increased or generated, or if the activity“glucoamylase” is increased or generated in an plant cell, plant or partthereof, especially with plastidic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.05-fold to 1.20-fold plus at least 100%thereof under low temperature conditions is conferred as compared to acorresponding non-transformed wild type plant cell, a plant or a partthereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6107, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6107 or a polypeptide SEQ ID NO. 6108, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6107 or polypeptide SEQ ID NO. 6108,respectively, is increased or generated, or if the activity “histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6150, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6150 or a polypeptide SEQ ID NO. 6151, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6150 or polypeptide SEQ ID NO. 6151,respectively, is increased or generated, or if the activity“saccharopine dehydrogenase” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 2.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6198, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6198 or a polypeptide SEQ ID NO. 6199, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6198 or polypeptide SEQ ID NO. 6199,respectively, is increased or generated, or if the activity “spindlecheckpoint complex subunit” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6208, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6208 or a polypeptide SEQ ID NO. 6209, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6208 or polypeptide SEQ ID NO. 6209,respectively, is increased or generated, or if the activity “nuclearpore complex subunit” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.41-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6242, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6242 or a polypeptide SEQ ID NO. 6243, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6242 or polypeptide SEQ ID NO. 6243,respectively, is increased or generated, or if the activity“yjl064w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.30-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6246, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6246 or a polypeptide SEQ ID NO. 6247, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6246 or polypeptide SEQ ID NO. 6247,respectively, is increased or generated, or if the activity“yjl067w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.29-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6250, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6250 or a polypeptide SEQ ID NO. 6251, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6250 or polypeptide SEQ ID NO. 6251,respectively, is increased or generated, or if the activity“potassium:hydrogen antiporter” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6297, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6297 or a polypeptide SEQ ID NO. 6298, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6297 or polypeptide SEQ ID NO. 6298,respectively, is increased or generated, or if the activity“GPI-anchored cell wall protein” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6326, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6326 or a polypeptide SEQ ID NO. 6327, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6326 or polypeptide SEQ ID NO. 6327,respectively, is increased or generated, or if the activity“yjl213w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.62-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.12-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6488, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6488 or a polypeptide SEQ ID NO. 6489, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6488 or polypeptide SEQ ID NO. 6489,respectively, is increased or generated, or if the activity“peptidyl-prolyl cis-trans isomerase” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.50-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6550, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6550 or a polypeptide SEQ ID NO. 6551, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6550 or polypeptide SEQ ID NO. 6551,respectively, is increased or generated, or if the activity “clathrinassociated protein complex small subunit” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.28-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.36-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6700, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6700 or a polypeptide SEQ ID NO. 6701, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6700 or polypeptide SEQ ID NO. 6701,respectively, is increased or generated, or if the activity “zincmetalloprotease” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.81-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.22-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 6816, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 6816 or a polypeptide SEQ ID NO. 6817, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 6816 or polypeptide SEQ ID NO. 6817,respectively, is increased or generated, or if the activity “F1F0 ATPsynthase beta subunit” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.52-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.37-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7366, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7366 or a polypeptide SEQ ID NO. 7367, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7366 or polypeptide SEQ ID NO. 7367,respectively, is increased or generated, or if the activity“alpha-mannosidase” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.52-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7475, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7475 or a polypeptide SEQ ID NO. 7476, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7475 or polypeptide SEQ ID NO. 7476,respectively, is increased or generated, or if the activity “ribosomalprotein of the small subunit” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.41-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7602, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7602 or a polypeptide SEQ ID NO. 7603, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7602 or polypeptide SEQ ID NO. 7603,respectively, is increased or generated, or if the activity“mitochondrial intermembrane space protein” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.20-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.10-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7651, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7651 or a polypeptide SEQ ID NO. 7652, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7651 or polypeptide SEQ ID NO. 7652,respectively, is increased or generated, or if the activity“phosphopantothenoylcysteine decarboxylase” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7661, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7661 or a polypeptide SEQ ID NO. 7662, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7661 or polypeptide SEQ ID NO. 7662,respectively, is increased or generated, or if the activity“ykl100c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7675, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7675 or a polypeptide SEQ ID NO. 7676, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7675 or polypeptide SEQ ID NO. 7676,respectively, is increased or generated, or if the activity“ykl131w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.22-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7679, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7679 or a polypeptide SEQ ID NO. 7680, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7679 or polypeptide SEQ ID NO. 7680,respectively, is increased or generated, or if the activity“mitochondrial ribosomal protein of the large subunit” is increased orgenerated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7710, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7710 or a polypeptide SEQ ID NO. 7711, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7710 or polypeptide SEQ ID NO. 7711,respectively, is increased or generated, or if the activity “G proteincoupled pheromone receptor receptor” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 2.69-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.57-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7735, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7735 or a polypeptide SEQ ID NO. 7736, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7735 or polypeptide SEQ ID NO. 7736,respectively, is increased or generated, or if the activity “golgimembrane protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.58-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.22-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7778, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7778 or a polypeptide SEQ ID NO. 7779, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7778 or polypeptide SEQ ID NO. 7779,respectively, is increased or generated, or if the activity “regulatorysubunit of Glc7p type 1 protein serine-threonine phosphatase” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.77-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 7829, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 7829 or a polypeptide SEQ ID NO. 7830, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 7829 or polypeptide SEQ ID NO. 7830,respectively, is increased or generated, or if the activity“dihydroorotate dehydrogenase” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 2.09-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8017, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8017 or a polypeptide SEQ ID NO. 8018, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8017 or polypeptide SEQ ID NO. 8018,respectively, is increased or generated, or if the activity“ykr016w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 2.00-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8045, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8045 or a polypeptide SEQ ID NO. 8046, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8045 or polypeptide SEQ ID NO. 8046,respectively, is increased or generated, or if the activity“ykr021w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 2.14-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8073, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8073 or a polypeptide SEQ ID NO. 8074, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8073 or polypeptide SEQ ID NO. 8074,respectively, is increased or generated, or if the activity“non-essential small GTPase of the Rho/Rac subfamily of Ras-likeproteins” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.57-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.09-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8263, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8263 or a polypeptide SEQ ID NO. 8264, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8263 or polypeptide SEQ ID NO. 8264,respectively, is increased or generated, or if the activity “integralmembrane protein localized to late Golgi vesicles” is increased orgenerated in an plant cell, plant or part thereof, especially withplastidic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.29-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.20-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8287, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8287 or a polypeptide SEQ ID NO. 8288, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8287 or polypeptide SEQ ID NO. 8288,respectively, is increased or generated, or if the activity “peptidetransporter” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 3.98-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8468, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8468 or a polypeptide SEQ ID NO. 8469, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8468 or polypeptide SEQ ID NO. 8469,respectively, is increased or generated, or if the activity“transcription factor” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.15-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.50-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8484, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8484 or a polypeptide SEQ ID NO. 8485, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8484 or polypeptide SEQ ID NO. 8485,respectively, is increased or generated, or if the activity“transmembrane protein with a role in cell wall polymer composition” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 4.43-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.12-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.30-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8492, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8492 or a polypeptide SEQ ID NO. 8493, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8492 or polypeptide SEQ ID NO. 8493,respectively, is increased or generated, or if the activity“yll014w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.61-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8514, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8514 or a polypeptide SEQ ID NO. 8515, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8514 or polypeptide SEQ ID NO. 8515,respectively, is increased or generated, or if the activity“non-essential Ras guanine nucleotide exchange factor” is increased orgenerated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8539, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8539 or a polypeptide SEQ ID NO. 8540, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8539 or polypeptide SEQ ID NO. 8540,respectively, is increased or generated, or if the activity“yll023c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.17-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8571, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8571 or a polypeptide SEQ ID NO. 8572, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8571 or polypeptide SEQ ID NO. 8572,respectively, is increased or generated, or if the activity“yll037w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.32-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8575, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8575 or a polypeptide SEQ ID NO. 8576, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8575 or polypeptide SEQ ID NO. 8576,respectively, is increased or generated, or if the activity“yll049w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.75-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8579, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8579 or a polypeptide SEQ ID NO. 8580, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8579 or polypeptide SEQ ID NO. 8580,respectively, is increased or generated, or if the activity “cysteinetransporter” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 5.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8661, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8661 or a polypeptide SEQ ID NO. 8662, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8661 or polypeptide SEQ ID NO. 8662,respectively, is increased or generated, or if the activity “metal iontransporter” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 4.38-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8991, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8991 or a polypeptide SEQ ID NO. 8992, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8991 or polypeptide SEQ ID NO. 8992,respectively, is increased or generated, or if the activity“ylr042c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.40-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8995, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8995 or a polypeptide SEQ ID NO. 8996, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8995 or polypeptide SEQ ID NO. 8996,respectively, is increased or generated, or if the activity“YLR053c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.55-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.17-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 8999, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 8999 or a polypeptide SEQ ID NO. 9000, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 8999 or polypeptide SEQ ID NO. 9000,respectively, is increased or generated, or if the activity “cytosolicserine hydroxymethyltransferase” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 9551, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 9551 or a polypeptide SEQ ID NO. 9552, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 9551 or polypeptide SEQ ID NO. 9552,respectively, is increased or generated, or if the activity “subunit ofcytoplasmic phenylalanyl-tRNA synthetase” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 3.72-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 9637, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 9637 or a polypeptide SEQ ID NO. 9638, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 9637 or polypeptide SEQ ID NO. 9638,respectively, is increased or generated, or if the activity“ylr065c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.88-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.24-fold plus at least 100%thereof under drought conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 9672, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 9672 or a polypeptide SEQ ID NO. 9673, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 9672 or polypeptide SEQ ID NO. 9673,respectively, is increased or generated, or if the activity “xylitoldehydrogenase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 2.66-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10182, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10182 or a polypeptide SEQ ID NO. 10183, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10182 or polypeptide SEQ ID NO. 10183,respectively, is increased or generated, or if the activity “3-ketosterol reductase” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.57-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10214, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10214 or a polypeptide SEQ ID NO. 10215, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10214 or polypeptide SEQ ID NO. 10215,respectively, is increased or generated, or if the activity “alkylhydroperoxide reductase” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.55-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10447, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10447 or a polypeptide SEQ ID NO. 10448, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10447 or polypeptide SEQ ID NO. 10448,respectively, is increased or generated, or if the activity“ylr25w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.28-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10451, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10451 or a polypeptide SEQ ID NO. 10452, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10451 or polypeptide SEQ ID NO. 10452,respectively, is increased or generated, or if the activity “anaphasepromoting complex (APC) subunit” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.22-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10463, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10463 or a polypeptide SEQ ID NO. 10464, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10463 or polypeptide SEQ ID NO. 10464,respectively, is increased or generated, or if the activity “proteincomponent of the large ribosomal subunit” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.14-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10533, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10533 or a polypeptide SEQ ID NO. 10534, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10533 or polypeptide SEQ ID NO. 10534,respectively, is increased or generated, or if the activity“mitochondrial protein” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.38-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10533, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10533 or a polypeptide SEQ ID NO. 10534, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10533 or polypeptide SEQ ID NO. 10534,respectively, is increased or generated, or if the activity“mitochondrial protein” is increased or generated in an plant cell,plant or part thereof, especially with plastidic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.05-fold to 1.22-fold plus at least 100%thereof under low temperature conditions is conferred as compared to acorresponding non-transformed wild type plant cell, a plant or a partthereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10541, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10541 or a polypeptide SEQ ID NO. 10542, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10541 or polypeptide SEQ ID NO. 10542,respectively, is increased or generated, or if the activity “ARV1protein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.61-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10562, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10562 or a polypeptide SEQ ID NO. 10563, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10562 or polypeptide SEQ ID NO. 10563,respectively, is increased or generated, or if the activity “GTP-bindingprotein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 2.75-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10990, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10990 or a polypeptide SEQ ID NO. 10991, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10990 or polypeptide SEQ ID NO. 10991,respectively, is increased or generated, or if the activity “proteininvolved in shmoo formation and bipolar bud site selection” is increasedor generated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 10998, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 10998 or a polypeptide SEQ ID NO. 10999, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 10998 or polypeptide SEQ ID NO. 10999,respectively, is increased or generated, or if the activity“non-essential kinetochore protein” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.54-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11004, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11004 or a polypeptide SEQ ID NO. 11005, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11004 or polypeptide SEQ ID NO. 11005,respectively, is increased or generated, or if the activity “Meioticrecombination protein” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.27-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11012, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11012 or a polypeptide SEQ ID NO. 11013, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11012 or polypeptide SEQ ID NO. 11013,respectively, is increased or generated, or if the activity “signaltransducing MEK kinase” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 3.40-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11054, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11054 or a polypeptide SEQ ID NO. 11055, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11054 or polypeptide SEQ ID NO. 11055,respectively, is increased or generated, or if the activity “cytochromec oxidase subunit VIII” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.56-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11066, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11066 or a polypeptide SEQ ID NO. 11067, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11066 or polypeptide SEQ ID NO. 11067,respectively, is increased or generated, or if the activity“ylr404w-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.33-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11074, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11074 or a polypeptide SEQ ID NO. 11075, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11074 or polypeptide SEQ ID NO. 11075,respectively, is increased or generated, or if the activity“ylr463c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.33-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11080, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11080 or a polypeptide SEQ ID NO. 11081, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11080 or polypeptide SEQ ID NO. 11081,respectively, is increased or generated, or if the activity “adeninephosphoribosyltransferase” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.27-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11552, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11552 or a polypeptide SEQ ID NO. 11553, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11552 or polypeptide SEQ ID NO. 11553,respectively, is increased or generated, or if the activity “Mcm1pbinding transcriptional repressor” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11569, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11569 or a polypeptide SEQ ID NO. 11570, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11569 or polypeptide SEQ ID NO. 11570,respectively, is increased or generated, or if the activity “originrecognition complex subunit” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.14-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11596, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11596 or a polypeptide SEQ ID NO. 11597, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11596 or polypeptide SEQ ID NO. 11597,respectively, is increased or generated, or if the activity“yml089c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.17-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11600, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11600 or a polypeptide SEQ ID NO. 11601, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11600 or polypeptide SEQ ID NO. 11601,respectively, is increased or generated, or if the activity“yml128c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.12-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 11612, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 11612 or a polypeptide SEQ ID NO. 11613, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 11612 or polypeptide SEQ ID NO. 11613,respectively, is increased or generated, or if the activity “hexosetransporter” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.52-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12246, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12246 or a polypeptide SEQ ID NO. 12247, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12246 or polypeptide SEQ ID NO. 12247,respectively, is increased or generated, or if the activity “Zinc fingerprotein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.41-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12263, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12263 or a polypeptide SEQ ID NO. 12264, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12263 or polypeptide SEQ ID NO. 12264,respectively, is increased or generated, or if the activity “proteinrequired for maturation of ribosomal RNAs” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 3.71-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12316, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12316 or a polypeptide SEQ ID NO. 12317, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12316 or polypeptide SEQ ID NO. 12317,respectively, is increased or generated, or if the activity “Factorarrest protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.28-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12327, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12327 or a polypeptide SEQ ID NO. 12328, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12327 or polypeptide SEQ ID NO. 12328,respectively, is increased or generated, or if the activity“YMR082C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.26-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12331, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12331 or a polypeptide SEQ ID NO. 12332, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12331 or polypeptide SEQ ID NO. 12332,respectively, is increased or generated, or if the activity “Nuclearcap-binding protein complex subunit” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12378, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12378 or a polypeptide SEQ ID NO. 12379, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12378 or polypeptide SEQ ID NO. 12379,respectively, is increased or generated, or if the activity “YMR126cmembrane protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12394, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12394 or a polypeptide SEQ ID NO. 12395, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12394 or polypeptide SEQ ID NO. 12395,respectively, is increased or generated, or if the activity“YMR144W-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.36-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12406, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12406 or a polypeptide SEQ ID NO. 12407, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12406 or polypeptide SEQ ID NO. 12407,respectively, is increased or generated, or if the activity“YMR160W-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.29-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12414, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12414 or a polypeptide SEQ ID NO. 12415, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12414 or polypeptide SEQ ID NO. 12415,respectively, is increased or generated, or if the activity “Stationaryphase protein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.51-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12420, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12420 or a polypeptide SEQ ID NO. 12421, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12420 or polypeptide SEQ ID NO. 12421,respectively, is increased or generated, or if the activity“YMR209C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.18-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12440, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12440 or a polypeptide SEQ ID NO. 12441, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12440 or polypeptide SEQ ID NO. 12441,respectively, is increased or generated, or if the activity“YMR233W-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.61-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12470, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12470 or a polypeptide SEQ ID NO. 12471, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12470 or polypeptide SEQ ID NO. 12471,respectively, is increased or generated, or if the activity“phosphoglucomutase/phosphomannomutase” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.20-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12749, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12749 or a polypeptide SEQ ID NO. 12750, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12749 or polypeptide SEQ ID NO. 12750,respectively, is increased or generated, or if the activity “RegulatoryCAT8 protein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.31-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12773, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12773 or a polypeptide SEQ ID NO. 12774, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12773 or polypeptide SEQ ID NO. 12774,respectively, is increased or generated, or if the activity“translational elongation factor EF-3 (HEF3)” is increased or generatedin an plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.11-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12829, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12829 or a polypeptide SEQ ID NO. 12830, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12829 or polypeptide SEQ ID NO. 12830,respectively, is increased or generated, or if the activity“YNL320W-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.46-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12883, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12883 or a polypeptide SEQ ID NO. 12884, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12883 or polypeptide SEQ ID NO. 12884,respectively, is increased or generated, or if the activity “Chitinsynthase 3 complex protein” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.15-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 12889, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 12889 or a polypeptide SEQ ID NO. 12890, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 12889 or polypeptide SEQ ID NO. 12890,respectively, is increased or generated, or if the activity“Alkyl/aryl-sulfatase” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 13014, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 13014 or a polypeptide SEQ ID NO. 13015, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 13014 or polypeptide SEQ ID NO. 13015,respectively, is increased or generated, or if the activity “antiviraladaptor protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.10-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 13018, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 13018 or a polypeptide SEQ ID NO. 13019, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 13018 or polypeptide SEQ ID NO. 13019,respectively, is increased or generated, or if the activity “repressorof G1 transcription” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.48-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 13024, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 13024 or a polypeptide SEQ ID NO. 13025, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 13024 or polypeptide SEQ ID NO. 13025,respectively, is increased or generated, or if the activity“YOR097c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.19-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 13030, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 13030 or a polypeptide SEQ ID NO. 13031, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 13030 or polypeptide SEQ ID NO. 13031,respectively, is increased or generated, or if the activity“Phosphoribosylaminoimidazole carboxylase” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.46-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 14085, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 14085 or a polypeptide SEQ ID NO. 14086, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14085 or polypeptide SEQ ID NO. 14086,respectively, is increased or generated, or if the activity “componentof the RAM signaling network” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.26-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 14093, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 14093 or a polypeptide SEQ ID NO. 14094, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14093 or polypeptide SEQ ID NO. 14094,respectively, is increased or generated, or if the activity “proteinkinase” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.33-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 14113, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 14113 or a polypeptide SEQ ID NO. 14114, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14113 or polypeptide SEQ ID NO. 14114,respectively, is increased or generated, or if the activity “signalrecognition particle subunit (SRP54)” is increased or generated in anplant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.61-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.26-fold plus at least 100%thereof under low temperature conditions; as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof.Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 14246, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 14246 or a polypeptide SEQ ID NO. 14247, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14246 or polypeptide SEQ ID NO. 14247,respectively, is increased or generated, or if the activity “regulatorysubunit of the 26S proteasome” is increased or generated in an plantcell, plant or part thereof, especially with cytoplasmic localization,an increase of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 14311, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 14311 or a polypeptide SEQ ID NO. 14312, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14311 or polypeptide SEQ ID NO. 14312,respectively, is increased or generated, or if the activity “RNApolymerase III subunit” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.22-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14914, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14914or a polypeptide SEQ ID NO. 14915, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14914 or polypeptide SEQ ID NO. 14915,respectively, is increased or generated, or if the activity“lysophospholipase” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15382, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15382 or a polypeptide SEQ ID NO. 15383, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15382 or polypeptide SEQ ID NO. 15383,respectively, is increased or generated, or if the activity“saccharopine dehydrogenase” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 2.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15460, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15460 or a polypeptide SEQ ID NO. 15461, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15460 or polypeptide SEQ ID NO. 15461,respectively, is increased or generated, or if the activity“alpha-mannosidase” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.52-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15571, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15571 or a polypeptide SEQ ID NO. 15572, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15571 or polypeptide SEQ ID NO. 15572,respectively, is increased or generated, or if the activity“ykl100c-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15593, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15593 or a polypeptide SEQ ID NO. 15594, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15593 or polypeptide SEQ ID NO. 15594,respectively, is increased or generated, or if the activity “regulatorysubunit of Glc7p type 1 protein serine-threonine phosphatase” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.77-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15646, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15646 or a polypeptide SEQ ID NO. 15647, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15646 or polypeptide SEQ ID NO. 15647,respectively, is increased or generated, or if the activity“non-essential Ras guanine nucleotide exchange factor” is increased orgenerated in an plant cell, plant or part thereof, especially withcytoplasmic localization, an increase of yield as compared to acorresponding non-transformed wild type plant cell, plant or a partthereof is conferred, especially an enhanced nutrient use efficiencyand/or an increased stress tolerance and/or an increased yield, in theabsence of a nutrient deficiency as well as stress conditions, inparticular an enhancement of NUE and/or an increase of biomassproduction as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof is conferred, or in particular anenhancement of NUE, or in particular an increase of biomass production,or an enhancement of NUE and an increase of biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15673, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15673 or a polypeptide SEQ ID NO. 15674, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15673 or polypeptide SEQ ID NO. 15674,respectively, is increased or generated, or if the activity “metal iontransporter” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 4.38-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16005, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16005 or a polypeptide SEQ ID NO. 16006, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16005 or polypeptide SEQ ID NO. 16006,respectively, is increased or generated, or if the activity “subunit ofcytoplasmic phenylalanyl-tRNA synthetase” is increased or generated inan plant cell, plant or part thereof, especially with cytoplasmiclocalization, an increase of yield as compared to a correspondingnon-transformed wild type plant cell, plant or a part thereof isconferred, especially an enhanced nutrient use efficiency and/or anincreased stress tolerance and/or an increased yield, in the absence ofa nutrient deficiency as well as stress conditions, in particular anenhancement of NUE and/or an increase of biomass production as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof is conferred, or in particular an enhancement of NUE, or inparticular an increase of biomass production, or an enhancement of NUEand an increase of biomass production.

Particularly, an increase from 1.1-fold to 3.72-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16114, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16114 or a polypeptide SEQ ID NO. 16115, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16114 or polypeptide SEQ ID NO. 16115,respectively, is increased or generated, or if the activity“YMR082C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.26-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14402, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14402or a polypeptide SEQ ID NO. 14403, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14402 or polypeptide SEQ ID NO. 14403,respectively, is increased or generated, or if the activity“B1258-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.36-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16093, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16093 or a polypeptide SEQ ID NO. 16094, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16093 or polypeptide SEQ ID NO. 16094,respectively, is increased or generated, or if the activity“YML101C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.35-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16106, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16106 or a polypeptide SEQ ID NO. 16107, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16106 or polypeptide SEQ ID NO. 16107,respectively, is increased or generated, or if the activity “nuclearfusion protein precursor” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.28-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16120, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16120 or a polypeptide SEQ ID NO. 16121, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16120 or polypeptide SEQ ID NO. 16121,respectively, is increased or generated, or if the activity “inheritanceof peroxisomes protein” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16275, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16275 or a polypeptide SEQ ID NO. 16276, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16275 or polypeptide SEQ ID NO. 16276,respectively, is increased or generated, or if the activity“exoribonuclease” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.16-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16305, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16305 or a polypeptide SEQ ID NO. 16306, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16305 or polypeptide SEQ ID NO. 16306,respectively, is increased or generated, or if the activity “iron sulfurcluster assembly protein” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.24-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16573, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16573 or a polypeptide SEQ ID NO. 16574, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16573 or polypeptide SEQ ID NO. 16574,respectively, is increased or generated, or if the activity“YPL068C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.11-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14396, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14396or a polypeptide SEQ ID NO. 14397, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14396 or polypeptide SEQ ID NO. 14397,respectively, is increased or generated, or if the activity“B0165-protein” is increased or generated in an plant cell, plant orpart thereof, especially with plastidic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.14-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.08-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.79-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16299, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16299 or a polypeptide SEQ ID NO. 16300, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16299 or polypeptide SEQ ID NO. 16300,respectively, is increased or generated, or if the activity“YOR203W-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.21-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16133, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16133 or a polypeptide SEQ ID NO. 16134, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16133 or polypeptide SEQ ID NO. 16134,respectively, is increased or generated, or if the activity“ribonucleoprotein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.15-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15056, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15056 or a polypeptide SEQ ID NO. 15057, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15056 or polypeptide SEQ ID NO. 15057,respectively, is increased or generated, or if the activity“transcription factor” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.11-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15587, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15587 or a polypeptide SEQ ID NO. 15588, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15587 or polypeptide SEQ ID NO. 15588,respectively, is increased or generated, or if the activity“YKL111C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.11-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16582, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16582 or a polypeptide SEQ ID NO. 16583, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16582 or polypeptide SEQ ID NO. 16583,respectively, is increased or generated, or if the activity “iron sulfurcluster assembly protein” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.13-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14839, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14839or a polypeptide SEQ ID NO. 14840, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14839 or polypeptide SEQ ID NO. 14840,respectively, is increased or generated, or if the activity “transportprotein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.16-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 15014, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 15014or a polypeptide SEQ ID NO. 15015, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15014 or polypeptide SEQ ID NO. 15015,respectively, is increased or generated, or if the activity “proteintranslocase protein” is increased or generated in an plant cell, plantor part thereof, especially with cytoplasmic localization, an increaseof yield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.42-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15432, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15432 or a polypeptide SEQ ID NO. 15433, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15432 or polypeptide SEQ ID NO. 15433,respectively, is increased or generated, or if the activity“YJL010C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.11-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.47-fold plus at least 100%thereof of yield in the absence of nutrient deficiency as well as stressconditions; as compared to a corresponding non-transformed wild typeplant cell, a plant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14497, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14497or a polypeptide SEQ ID NO. 14498, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14497 or polypeptide SEQ ID NO. 14498,respectively, is increased or generated, or if the activity“B1267-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.23-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; ascompared to a corresponding non-transformed wild type plant cell, aplant or a part thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14718, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14718or a polypeptide SEQ ID NO. 14719, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14718 or polypeptide SEQ ID NO. 14719,respectively, is increased or generated, or if the activity “membraneprotein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.33-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.06-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.20-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14791, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14791or a polypeptide SEQ ID NO. 14792, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14791 or polypeptide SEQ ID NO. 14792,respectively, is increased or generated, or if the activity“B1381-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.11-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Escherichia coli nucleicacid molecule SEQ ID NO. 14879, or the activity of a polypeptide encodedby a nucleic acid molecule comprising the nucleic acid SEQ ID NO. 14879or a polypeptide SEQ ID NO. 14880, respectively, is increased orgenerated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 14879 or polypeptide SEQ ID NO. 14880,respectively, is increased or generated, or if the activity“B2646-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.31-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.11-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.23-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15064, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15064 or a polypeptide SEQ ID NO. 15065, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15064 or polypeptide SEQ ID NO. 15065,respectively, is increased or generated, or if the activity “60Sribosomal protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.12-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15257, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15257 or a polypeptide SEQ ID NO. 15258, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15257 or polypeptide SEQ ID NO. 15258,respectively, is increased or generated, or if the activity “RhoGDP-dissociation inhibitor” is increased or generated in an plant cell,plant or part thereof, especially with cytoplasmic localization, anincrease of yield as compared to a corresponding non-transformed wildtype plant cell, plant or a part thereof is conferred, especially anenhanced nutrient use efficiency and/or an increased stress toleranceand/or an increased yield, in the absence of a nutrient deficiency aswell as stress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.33-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 15378, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 15378 or a polypeptide SEQ ID NO. 15379, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 15378 or polypeptide SEQ ID NO. 15379,respectively, is increased or generated, or if the activity“YHL005C-protein” is increased or generated in an plant cell, plant orpart thereof, especially with cytoplasmic localization, an increase ofyield as compared to a corresponding non-transformed wild type plantcell, plant or a part thereof is conferred, especially an enhancednutrient use efficiency and/or an increased stress tolerance and/or anincreased yield, in the absence of a nutrient deficiency as well asstress conditions, in particular an enhancement of NUE and/or anincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, a plant or a part thereof isconferred, or in particular an enhancement of NUE, or in particular anincrease of biomass production, or an enhancement of NUE and an increaseof biomass production.

Particularly, an increase from 1.1-fold to 1.25-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16629, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16629 or a polypeptide SEQ ID NO. 16630, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16629 or polypeptide SEQ ID NO. 16630,respectively, is increased or generated, or if the activity“transmembrane protein with a role in cell wall polymer composition” isincreased or generated in an plant cell, plant or part thereof,especially with cytoplasmic localization, an increase of yield ascompared to a corresponding non-transformed wild type plant cell, plantor a part thereof is conferred, especially an enhanced nutrient useefficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 4.43-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred; alsoparticularly, an increase from 1.05-fold to 1.12-fold plus at least 100%thereof under low temperature conditions; also particularly, an increasefrom 1.05-fold to 1.30-fold plus at least 100% thereof of yield in theabsence of nutrient deficiency as well as stress conditions; as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

Accordingly, in one embodiment, in case the Saccharomyces cerevisiaenucleic acid molecule SEQ ID NO. 16647, or the activity of a polypeptideencoded by a nucleic acid molecule comprising the nucleic acid SEQ IDNO. 16647 or a polypeptide SEQ ID NO. 16648, respectively, is increasedor generated, e.g. if the activity of such a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 16647 or polypeptide SEQ ID NO. 16648,respectively, is increased or generated, or if the activity “Stationaryphase protein” is increased or generated in an plant cell, plant or partthereof, especially with cytoplasmic localization, an increase of yieldas compared to a corresponding non-transformed wild type plant cell,plant or a part thereof is conferred, especially an enhanced nutrientuse efficiency and/or an increased stress tolerance and/or an increasedyield, in the absence of a nutrient deficiency as well as stressconditions, in particular an enhancement of NUE and/or an increase ofbiomass production as compared to a corresponding non-transformed wildtype plant cell, a plant or a part thereof is conferred, or inparticular an enhancement of NUE, or in particular an increase ofbiomass production, or an enhancement of NUE and an increase of biomassproduction.

Particularly, an increase from 1.1-fold to 1.51-fold plus at least 100%thereof under conditions of nitrogen deficiency is conferred as comparedto a corresponding non-transformed wild type plant cell, a plant or apart thereof.

The ratios indicated above particularly refer to an increased yieldactually measured as increase of biomass, especially as fresh weightbiomass of aerial parts.

For the purposes of the invention, as a rule the plural is intended toencompass the singular and vice versa.

Unless otherwise specified, the terms “polynucleotides”, “nucleic acid”and “nucleic acid molecule” are interchangeably in the present context.Unless otherwise specified, the terms “peptide”, “polypeptide” and“protein” are interchangeably in the present context. The term“sequence” may relate to polynucleotides, nucleic acids, nucleic acidmolecules, peptides, polypeptides and proteins, depending on the contextin which the term “sequence” is used. The terms “gene(s)”,“polynucleotide”, “nucleic acid sequence”, “nucleotide sequence”, or“nucleic acid molecule(s)” as used herein refers to a polymeric form ofnucleotides of any length, either ribonucleotides ordeoxyribonucleotides. The terms refer only to the primary structure ofthe molecule.

Thus, the terms “gene(s)”, “polynucleotide”, “nucleic acid sequence”,“nucleotide sequence”, or “nucleic acid molecule(s)” as used hereininclude double- and single-stranded DNA and/or RNA. They also includeknown types of modifications, for example, methylation, “caps”,substitutions of one or more of the naturally occurring nucleotides withan analog. Preferably, the DNA or RNA sequence comprises a codingsequence encoding the herein defined polypeptide.

A “coding sequence” is a nucleotide sequence, which is transcribed intoan RNA, e.g. a regulatory RNA, such as a miRNA, a ta-siRNA,cosuppression molecule, an RNAi, a ribozyme, etc. or into a mRNA whichis translated into a polypeptide when placed under the control ofappropriate regulatory sequences. The boundaries of the coding sequenceare determined by a translation start codon at the 5′-terminus and atranslation stop codon at the 3′-terminus. The tripletts taa, tga andtag represent the (usual) stop codons which are interchangeable. Acoding sequence can include, but is not limited to mRNA, cDNA,recombinant nucleotide sequences or genomic DNA, while introns may bepresent as well under certain circumstances.

As used in the present context a nucleic acid molecule may alsoencompass the untranslated sequence located at the 3′ and at the 5′ endof the coding gene region, for example at least 500, preferably 200,especially preferably 100, nucleotides of the sequence upstream of the5′ end of the coding region and at least 100, preferably 50, especiallypreferably 20, nucleotides of the sequence downstream of the 3′ end ofthe coding gene region. In the event for example the antisense, RNAi,snRNA, dsRNA, siRNA, miRNA, ta-siRNA, cosuppression molecule, ribozymeetc. technology is used coding regions as well as the 5′- and/or3′-regions can advantageously be used. However, it is often advantageousonly to choose the coding region for cloning and expression purposes.

“Polypeptide” refers to a polymer of amino acid (amino acid sequence)and does not refer to a specific length of the molecule. Thus, peptidesand oligopeptides are included within the definition of polypeptide.This term does also refer to or include posttranslational modificationsof the polypeptide, for example, glycosylations, acetylations,phosphorylations and the like. Included within the definition are, forexample, polypeptides containing one or more analogs of an amino acid(including, for example, unnatural amino acids, etc.), polypeptides withsubstituted linkages, as well as other modifications known in the art,both naturally occurring and non-naturally occurring.

The term “table I” used in this specification is to be taken to specifythe content of table I A and table I B. The term “table II” used in thisspecification is to be taken to specify the content of table II A andtable II B. The term “table I A” used in this specification is to betaken to specify the content of table I A. The term “table I B” used inthis specification is to be taken to specify the content of table I B.The term “table II A” used in this specification is to be taken tospecify the content of table II A. The term “table II B” used in thisspecification is to be taken to specify the content of table II B. Inone preferred embodiment, the term “table I” means table I B. In onepreferred embodiment, the term “table II” means table II B.

The terms “comprise” or “comprising” and grammatical variations thereofwhen used in this specification are to be taken to specify the presenceof stated features, integers, steps or components or groups thereof, butnot to preclude the presence or addition of one or more other features,integers, steps, components or groups thereof.

In accordance with the invention, a protein or polypeptide has the“activity of an protein as shown in table II, column 3” if its de novoactivity, or its increased expression directly or indirectly leads toand confers an increased yield, especially an enhanced NUE and/orincreased biomass production, as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof and theprotein has the above mentioned activities of a protein as shown intable II, column 3. Throughout the specification the activity orpreferably the biological activity of such a protein or polypeptide oran nucleic acid molecule or sequence encoding such protein orpolypeptide is identical or similar if it still has the biological orenzymatic activity of a protein as shown in table II, column 3, or whichhas at least 10% of the original enzymatic activity, preferably 20%,30%, 40%, 50%, particularly preferably 60%, 70%, 80% most particularlypreferably 90%, 95%, 98%, 99% in comparison to a protein as shown intable II, column 3 of E. coli or Saccharomyces cerevisiae. In anotherembodiment the biological or enzymatic activity of a protein as shown intable II, column 3, has at least 101% of the original enzymaticactivity, preferably 110%, 120%, %, 150%, particularly preferably 150%,200%, 300% in comparison to a protein as shown in table II, column 3 ofE. coli or Saccharomyces cerevisiae.

The terms “increased”, “raised”, “extended”, “enhanced”, “improved” or“amplified” relate to a corresponding change of a property in a plant,an organism, a part of an organism such as a tissue, seed, root, leave,flower etc. or in a cell and are interchangeable. Preferably, theoverall activity in the volume is increased or enhanced in cases if theincrease or enhancement is related to the increase or enhancement of anactivity of a gene product, independent whether the amount of geneproduct or the specific activity of the gene product or both isincreased or enhanced or whether the amount, stability or translationefficacy of the nucleic acid sequence or gene encoding for the geneproduct is increased or enhanced.

The terms “increase” relate to a corresponding change of a property anorganism or in a part of a plant, an organism, such as a tissue, seed,root, leave, flower etc. or in a cell. Preferably, the overall activityin the volume is increased in cases the increase relates to the increaseof an activity of a gene product, independent whether the amount of geneproduct or the specific activity of the gene product or both isincreased or generated or whether the amount, stability or translationefficacy of the nucleic acid sequence or gene encoding for the geneproduct is increased.

Under “change of a property” it is understood that the activity,expression level or amount of a gene product or the metabolite contentis changed in a specific volume relative to a corresponding volume of acontrol, reference or wild type, including the de novo creation of theactivity or expression.

The terms “increase” include the change of said property in only partsof the subject of the present invention, for example, the modificationcan be found in compartment of a cell, like a organelle, or in a part ofa plant, like tissue, seed, root, leave, flower etc. but is notdetectable if the overall subject, i.e. complete cell or plant, istested.

Accordingly, the term “increase” means that the specific activity of anenzyme as well as the amount of a compound or metabolite, e.g. of apolypeptide, a nucleic acid molecule of the invention or an encodingmRNA or DNA, can be increased in a volume.

The terms “wild type”, “control” or “reference” are exchangeable and canbe a cell or a part of organisms such as an organelle like a chloroplastor a tissue, or an organism, in particular a plant, which was notmodified or treated according to the herein described process accordingto the invention. Accordingly, the cell or a part of organisms such asan organelle like a chloroplast or a tissue, or an organism, inparticular a plant used as wild type, control or reference correspondsto the cell, organism, plant or part thereof as much as possible and isin any other property but in the result of the process of the inventionas identical to the subject matter of the invention as possible. Thus,the wild type, control or reference is treated identically or asidentical as possible, saying that only conditions or properties mightbe different which do not influence the quality of the tested property.

Preferably, any comparison is carried out under analogous conditions.The term “analogous conditions” means that all conditions such as, forexample, culture or growing conditions, soil, nutrient, water content ofthe soil, temperature, humidity or surrounding air or soil, assayconditions (such as buffer composition, temperature, substrates,pathogen strain, concentrations and the like) are kept identical betweenthe experiments to be compared.

The “reference”, “control”, or “wild type” is preferably a subject, e.g.an organelle, a cell, a tissue, an organism, in particular a plant,which was not modified or treated according to the herein describedprocess of the invention and is in any other property as similar to thesubject matter of the invention as possible. The reference, control orwild type is in its genome, transcriptome, proteome or metabolome assimilar as possible to the subject of the present invention. Preferably,the term “reference-” “control-” or “wild type-”-organelle, -cell,-tissue or -organism, in particular plant, relates to an organelle,cell, tissue or organism, in particular plant, which is nearlygenetically identical to the organelle, cell, tissue or organism, inparticular plant, of the present invention or a part thereof preferably95%, more preferred are 98%, even more preferred are 99.00%, inparticular 99,10%, 99,30%, 99.50%, 99,70%, 99,90%, 99,99%, 99,999% ormore. Most preferable the “reference”, “control”, or “wild type” is asubject, e.g. an organelle, a cell, a tissue, an organism, in particulara plant, which is genetically identical to the organism, in particularplant, cell, a tissue or organelle used according to the process of theinvention except that the responsible or activity conferring nucleicacid molecules or the gene product encoded by them are amended,manipulated, exchanged or introduced according to the inventive process.

In case, a control, reference or wild type differing from the subject ofthe present invention only by not being subject of the process of theinvention can not be provided, a control, reference or wild type can bean organism in which the cause for the modulation of an activityconferring the enhanced NUE and/or increased biomass production forexample as compared to a corresponding non-transformed wild type plantcell, plant or part thereof or expression of the nucleic acid moleculeof the invention as described herein has been switched back or off, e.g.by knocking out the expression of responsible gene product, e.g. byantisense inhibition, by inactivation of an activator or agonist, byactivation of an inhibitor or antagonist, by inhibition through addinginhibitory antibodies, by adding active compounds as e.g. hormones, byintroducing negative dominant mutants, etc. A gene production can forexample be knocked out by introducing inactivating point mutations,which lead to an enzymatic activity inhibition or a destabilization oran inhibition of the ability to bind to cofactors etc.

Accordingly, preferred reference subject is the starting subject of thepresent process of the invention. Preferably, the reference and thesubject matter of the invention are compared after standardization andnormalization, e.g. to the amount of total RNA, DNA, or protein oractivity or expression of reference genes, like housekeeping genes, suchas ubiquitin, actin or ribosomal proteins.

The increase or modulation according to this invention can beconstitutive, e.g. due to a stable permanent transgenic expression or toa stable mutation in the corresponding endogenous gene encoding thenucleic acid molecule of the invention or to a modulation of theexpression or of the behavior of a gene conferring the expression of thepolypeptide of the invention, or transient, e.g. due to an transienttransformation or temporary addition of a modulator such as a agonist orantagonist or inducible, e.g. after transformation with a inducibleconstruct carrying the nucleic acid molecule of the invention undercontrol of a inducible promoter and adding the inducer, e.g.tetracycline or as described herein below.

The increase in activity of the polypeptide amounts in a cell, a tissue,an organelle, an organ or an organism, preferably a plant, or a partthereof preferably to at least 5%, preferably to at least 20% or at toleast 50%, especially preferably to at least 70%, 80%, 90% or more, veryespecially preferably are to at least 100%, 150% or 200%, mostpreferably are to at least 250% or more in comparison to the control,reference or wild type.

In one embodiment the term increase means the increase in amount inrelation to the weight of the organism or part thereof (w/w).

In one embodiment the increase in activity of the polypeptide amounts inan organelle such as a plastid.

In another embodiment the increase in activity of the polypeptideamounts in the cytosol.

The specific activity of a polypeptide encoded by a nucleic acidmolecule of the present invention or of the polypeptide of the presentinvention can be tested as described in the examples. In particular, theexpression of a protein in question in a cell, e.g. a plant cell incomparison to a control is an easy test and can be performed asdescribed in the state of the art.

The term “increase” includes, that a compound or an activity, especiallyan activity, is introduced into a cell, the cytosol or a subcellularcompartment or organelle de novo or that the compound or the activity,especially an activity, has not been detected before, in other words itis “generated”.

Accordingly, in the following, the term “increasing” also comprises theterm “generating” or “stimulating”. The increased activity manifestsitself in an increased yield, especially an enhanced NUE and/orincreased biomass production, as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof.

The sequence of B0017 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b0017-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b0017-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0017 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0017; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown n column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0017 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0017,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b0017-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b0017-protein”, is increased cytoplasmic.

The sequence of B0045 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as transport protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transport protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0045 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0045; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0045 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0045,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transport protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transport protein”, is increasedcytoplasmic.

The sequence of B0180 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as hydroxymyristol acyl carrier proteindehydratase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “hydroxymyristol acyl carrier protein dehydratase”from Escherichia coli or its functional equivalent or its homolog, e.g.the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0180 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0180; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0180 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0180,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “hydroxymyristol acyl carrier proteindehydratase”, preferably it is the molecule of section (a) or (b) ofthis paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “hydroxymyristol acyl carrier proteindehydratase”, is increased plastidic.

The sequence of B0242 from Escherichia coli K12, e.g. as shown in column5 of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as gamma-glutamyl kinase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “gamma-glutamyl kinase” from Escherichia coli K12 orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0242 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0242; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0242 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0242,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “gamma-glutamyl kinase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “gamma-glutamyl kinase”, is increasedplastidic.

The sequence of B0403 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as alpha-glucosidase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “alpha-glucosidase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0403 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0403; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0403 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0403,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “alpha-glucosidase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “alpha-glucosidase”, is increased plastidic.

The sequence of B0474 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as adenylate kinase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “adenylate kinase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0474 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0474; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0474 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0474,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “adenylate kinase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “adenylate kinase”, is increased cytoplasmic.

The sequence of B0754 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as 2-dehydro-3-deoxy-phosphoheptonatealdolase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “2-dehydro-3-deoxy-phosphoheptonate aldolase” fromEscherichia coli or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0754 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0754; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0754 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0754,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “2-dehydro-3-deoxy-phosphoheptonatealdolase”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “2-dehydro-3-deoxy-phosphoheptonatealdolase”, is increased plastidic.

The sequence of B0784 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as molybdopterin biosynthesis protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “molybdopterin biosynthesis protein” from Escherichiacoli or its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0784 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0784; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0784 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0784,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “molybdopterin biosynthesis protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “molybdopterin biosynthesis protein”, isincreased cytoplasmic.

The sequence of B0873 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as hydroxylamine reductase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “hydroxylamine reductase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0873 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0873; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0873 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0873,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “hydroxylamine reductase”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “hydroxylamine reductase”, is increasedplastidic.

The sequence of B1014 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as proline dehydrogenase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “proline dehydrogenase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1014 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1014; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1014 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1014,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “proline dehydrogenase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “proline dehydrogenase”, is increasedcytoplasmic.

The sequence of B1020 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as PhoH-like protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “PhoH-like protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1020 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1020; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1020 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1020,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “PhoH-like protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “PhoH-like protein”, is increased plastidic.

The sequence of B1180 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as isomerase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “isomerase” from Escherichia coli or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1180 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1180; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1180 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1180,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “isomerase”, preferably it is the molecule ofsection (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “isomerase”, is increased cytoplasmic.

The sequence of B1933 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b1933-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b1933-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1933 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1933; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1933 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1933,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b1933-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b1933-protein”, is increased plastidic.

The sequence of B2032 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as glycosyltransferase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “glycosyltransferase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2032 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2032; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2032 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2032,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “glycosyltransferase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “glycosyltransferase”, is increasedplastidic.

The sequence of B2165 from Escherichia coli K12, e.g. as shown in column5 of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b2165-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b2165-protein” from Escherichia coli K12 or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2165 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2165; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2165 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2165,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b2165-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b2165-protein”, is increased plastidic.

The sequence of B2223 from Escherichia coli K12, e.g. as shown in column5 of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as short chain fatty acid transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “short chain fatty acid transporter” from Escherichiacoli K12 or its functional equivalent or its homolog, e.g. the increaseof

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2223 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2223; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2223 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2223,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “short chain fatty acid transporter”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “short chain fatty acid transporter”, isincreased plastidic.

The sequence of B2238 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b2238-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b2238-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2238 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2238; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2238 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2238,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b2238-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b2238-protein”, is increased plastidic.

In another embodiment, said molecule, which activity is to be increasedin the process of the invention and which is the gene product with anactivity as described as a “b2238-protein”, is increased cytoplasmic.

The sequence of B2310 from Escherichia coli K12, e.g. as shown in column5 of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as lysine/arginine/ornithine transportersubunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “lysine/arginine/ornithine transporter subunit” fromEscherichia coli K12 or its functional equivalent or its homolog, e.g.the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2310 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2310; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2310 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2310,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “lysine/arginine/ornithine transportersubunit”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “lysine/arginine/ornithine transportersubunit”, is increased plastidic.

The sequence of B2431 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b2431-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b2431-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2431 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2431; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2431 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2431,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b2431-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b2431-protein”, is increased plastidic.

The sequence of B2600 from Escherichia coli K12, e.g. as shown in column5 of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as chorismate mutase T/prephenatedehydrogenase (bifunctional).

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “chorismate mutase T/prephenate dehydrogenase(bifunctional)” from Escherichia coli K12 or its functional equivalentor its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2600 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2600; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2600 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2600,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “chorismate mutase T/prephenate dehydrogenase(bifunctional)”, preferably it is the molecule of section (a) or (b) ofthis paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “chorismate mutase T/prephenate dehydrogenase(bifunctional)”, is increased plastidic.

The sequence of B2766 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b2766-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b2766-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2766 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2766; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2766 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2766,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b2766-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b2766-protein”, is increased plastidic.

The sequence of B2903 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as glycine decarboxylase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “glycine decarboxylase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2903 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2903; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2903 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2903,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “glycine decarboxylase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “glycine decarboxylase”, is increasedcytoplasmic.

The sequence of B3117 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as threonine ammonia-lyase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “threonine ammonia-lyase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3117 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3117; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3117 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3117,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “threonine ammonia-lyase”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “threonine ammonia-lyase”, is increasedplastidic.

The sequence of B3120 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as b3120-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “b3120-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3120 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3120; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3120 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3120,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “b3120-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “b3120-protein”, is increased plastidic.

The sequence of B3216 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as outer membrane usher protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “outer membrane usher protein” from Escherichia colior its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3216 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3216; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3216 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3216,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “outer membrane usher protein”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “outer membrane usher protein”, is increasedplastidic.

The sequence of B3451 from Escherichia coli K12, e.g. as shown in column5 of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as glycerol-3-phosphate transporter subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “glycerol-3-phosphate transporter subunit” fromEscherichia coli K12 or its functional equivalent or its homolog, e.g.the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3451 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3451; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3451 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3451,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “glycerol-3-phosphate transporter subunit”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “glycerol-3-phosphate transporter subunit”,is increased plastidic.

The sequence of B3791 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as hydro-lyase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “hydro-lyase” from Escherichia coli or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3791 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3791; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3791 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3791,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “hydrolyase”, preferably it is the moleculeof section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “hydrolyase”, is increased cytoplasmic.

The sequence of B3825 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as lysophospholipase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “lysophospholipase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3825 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3825; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3825 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3825,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “lysophospholipase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “lysophospholipase”, is increased plastidic.

The sequence of Yal019w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yal019w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yal019w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yal019w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yal019w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yal019w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yal019w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yal019w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yal019w-protein”, is increased cytoplasmic.

The sequence of Yar035w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as carnitine acetyltransferase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “carnitine acetyltransferase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yar035w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yar035w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yar035w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yar035w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “carnitine acetyltransferase”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “carnitine acetyltransferase”, is increasedcytoplasmic.

The sequence of Ybl021c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Transcriptional activator.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Transcriptional activator” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ybl021c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ybl021c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table I or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ybl021c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ybl021c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Transcriptional activator”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Transcriptional activator”, is increasedcytoplasmic.

The sequence of Ybr055c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as splicing factor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “splicing factor” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ybr055c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ybr055c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ybr055c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ybr055c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “splicing factor”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “splicing factor”, is increased cytoplasmic.

The sequence of YBR128C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as autophagy-specificphosphatidylinositol 3-kinase complex protein subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit” from Saccharomyces cerevisiae or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YBR128C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YBR128C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YBR128C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YBR128C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “autophagy-specific phosphatidylinositol3-kinase complex protein subunit”, preferably it is the molecule ofsection (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “autophagy-specific phosphatidylinositol3-kinase complex protein subunit”, is increased cytoplasmic.

The sequence of Ybr159w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as microsomal beta-ketoreductase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “microsomal beta-keto-reductase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ybr159w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ybr159w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ybr159w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ybr159w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “microsomal beta-keto-reductase”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “microsomal beta-keto-reductase”, isincreased cytoplasmic.

The sequence of Ybr243c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as UDP-N-acetyl-glucosamine-1-Ptransferase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “UDP-N-acetyl-glucosamine-1-P transferase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ybr243c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ybr243c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ybr243c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ybr243c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “UDP-N-acetyl-glucosamine-1-P transferase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “UDP-N-acetyl-glucosamine-1-P transferase”,is increased cytoplasmic.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “UDP-N-acetyl-glucosamine-1-P transferase”,is increased plastidic.

The sequence of Ybr262c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ybr262c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ybr262c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ybr262c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ybr262c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ybr262c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ybr262c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ybr262c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ybr262c-protein”, is increased cytoplasmic.

The sequence of Ycr019w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as protein necessary for structuralstability of L-A double-stranded RNA-containing particles.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein necessary for structural stability of L-Adouble-stranded RNA-containing particles” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ycr019w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ycr019w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ycr019w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ycr019w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein necessary for structural stabilityof L-A double-stranded RNA-containing particles”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein necessary for structural stabilityof L-A double-stranded RNA-containing particles”, is increasedcytoplasmic.

The sequence of Ydr070c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YDR070C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YDR070C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr070c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr070c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr070c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr070c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YDR070C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YDR070C-protein”, is increased cytoplasmic.

The sequence of Ydr079w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as chaperone.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “chaperone” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr079w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr079w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr079w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr079w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “chaperone”, preferably it is the molecule ofsection (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “chaperone”, is increased cytoplasmic.

The sequence of Ydr123c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as helix-loop-helix transcriptionactivator that binds inositol/choline-responsive elements.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “helix-loop-helix transcription activator that bindsinositol/choline-responsive elements” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr123c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr123c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr123c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr123c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “helix-loop-helix transcription activatorthat binds inositol/choline-responsive elements”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “helix-loop-helix transcription activatorthat binds inositol/choline-responsive elements”, is increasedcytoplasmic.

The sequence of Ydr137w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as golgi membrane exchange factorsubunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “golgi membrane exchange factor subunit” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr137w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr137w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr137w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr137w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “golgi membrane exchange factor subunit”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “golgi membrane exchange factor subunit”, isincreased cytoplasmic.

The sequence of Ydr294c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as dihydrosphingosine phosphate lyase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “dihydrosphingosine phosphate lyase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr294c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr294c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr294c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr294c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “dihydrosphingosine phosphate lyase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “dihydrosphingosine phosphate lyase”, isincreased cytoplasmic.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “dihydrosphingosine phosphate lyase”, isincreased plastidic.

The sequence of Ydr330w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ubiquitin regulatory protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ubiquitin regulatory protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr330w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr330w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr330w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr330w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ubiquitin regulatory protein”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ubiquitin regulatory protein”, is increasedcytoplasmic.

The sequence of Ydr355c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ydr355c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ydr355c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr355c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr355c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr355c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr355c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ydr355c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ydr355c-protein”, is increased cytoplasmic.

The sequence of YDR430C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as lysine-specific metalloprotease.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “lysine-specific metalloprotease” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YDR430C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YDR430C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YDR430C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YDR430C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “lysine-specific metalloprotease”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “lysine-specific metalloprotease”, isincreased plastidic.

The sequence of Ydr472w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as subunit of the transport proteinparticle (TRAPP) complex of the cis-Golgi.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “subunit of the transport protein particle (TRAPP)complex of the cis-Golgi” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ydr472w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ydr472w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ydr472w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ydr472w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “subunit of the transport protein particle(TRAPP) complex of the cis-Golgi”, preferably it is the molecule ofsection (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “subunit of the transport protein particle(TRAPP) complex of the cis-Golgi”, is increased cytoplasmic.

The sequence of YDR497C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as myo-inositol transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “myo-inositol transporter” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YDR497C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YDR497C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YDR497C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YDR497C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “myo-inositol transporter”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “myo-inositol transporter”, is increasedplastidic.

The sequence of Yer029c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as SM complex B protein for mRNAsplicing.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “SM complex B protein for mRNA splicing” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yer029c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yer029c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yer029c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yer029c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “SM complex B protein for mRNA splicing”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “SM complex B protein for mRNA splicing”, isincreased cytoplasmic.

The sequence of YFR007W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YFR007W-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YFR007W-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YFR007W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YFR007W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YFR007W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YFR007W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YFR007W-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YFR007W-protein”, is increased cytoplasmic.

The sequence of YGL039W from Saccharomyces cerevisiae, e.g. as shown incolumn of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as oxidoreductase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “oxidoreductase” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YGL039W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YGL039W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YGL039W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YGL039W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “oxidoreductase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “oxidoreductase”, is increased cytoplasmic.

The sequence of Ygl043w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as transcription elongation factor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transcription elongation factor” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygl043w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygl043w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygl043w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygl043w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transcription elongation factor”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transcription elongation factor”, isincreased cytoplasmic.

The sequence of Ygr088w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as cytosolic catalase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “cytosolic catalase” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr088w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr088w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr088w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr088w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “cytosolic catalase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “cytosolic catalase”, is increasedcytoplasmic.

The sequence of Ygr122c-a from Saccharomyces cerevisiae, e.g. as shownin column 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ygr122c-a-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ygr122c-a-protein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr122c-a or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr122c-a; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr122c-a or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Ygr122c-a,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ygr122c-a-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ygr122c-a-protein”, is increasedcytoplasmic.

The sequence of Ygr142w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as v-SNARE binding protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “v-SNARE binding protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr142w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr142w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr142w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr142w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “v-SNARE binding protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “v-SNARE binding protein”, is increasedcytoplasmic.

The sequence of Ygr143w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as protein involved in sphingolipidbiosynthesis.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein involved in sphingolipid biosynthesis” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr143w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr143w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr143w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr143w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein involved in sphingolipidbiosynthesis”, preferably it is the molecule of section (a) or (b) ofthis paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein involved in sphingolipidbiosynthesis”, is increased cytoplasmic.

The sequence of Ygr165w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as mitochondrial ribosomal protein ofthe small subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “mitochondrial ribosomal protein of the small subunit”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr165w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr165w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr165w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr165w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “mitochondrial ribosomal protein of the smallsubunit”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “mitochondrial ribosomal protein of the smallsubunit”, is increased cytoplasmic.

The sequence of Ygr170w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as phosphatidylserine decarboxylase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “phosphatidylserine decarboxylase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr170w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr170w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr170w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr170w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “phosphatidylserine decarboxylase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “phosphatidylserine decarboxylase”, isincreased cytoplasmic.

The sequence of Ygr202c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as cholinephosphatecytidylyltransferase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “cholinephosphate cytidylyltransferase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr202c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr202c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr202c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr202c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “cholinephosphate cytidylyltransferase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “cholinephosphate cytidylyltransferase”, isincreased cytoplasmic.

The sequence of Ygr266w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ygr266w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ygr266w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr266w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr266w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr266w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr266w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ygr266w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ygr266w-protein”, is increased cytoplasmic.

The sequence of Ygr282c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as cell wall endo-beta-1,3-glucanase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “cell wall endo-beta-1,3-glucanase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr282c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr282c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr282c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr282c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “cell wall endo-beta-1,3-glucanase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “cell wall endo-beta-1,3-glucanase”, isincreased cytoplasmic.

The sequence of Ygr290w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ygr290w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ygr290w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ygr290w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ygr290w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ygr290w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ygr290w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ygr290w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ygr290w-protein”, is increased cytoplasmic.

The sequence of Yhl021c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yhl021c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yhl021c-protein”from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yhl021c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yhl021c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yhl021c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yhl021c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yhl021c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yhl021c-protein”, is increased cytoplasmic.

The sequence of Yhl031c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as v-SNARE protein involved in Golgitransport.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “v-SNARE protein involved in Golgi transport” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yhl031c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yhl031c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yhl031c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yhl031c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “v-SNARE protein involved in Golgitransport”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “v-SNARE protein involved in Golgitransport”, is increased cytoplasmic.

The sequence of Yhr011w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as mitochondrial seryl-tRNA synthetase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “mitochondrial seryl-tRNA synthetase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yhr011w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yhr011w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yhr011w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yhr011w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “mitochondrial seryl-tRNA synthetase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “mitochondrial seryl-tRNA synthetase”, isincreased cytoplasmic.

The sequence of Yhr127w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yhr127w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yhr127w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yhr127w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yhr127w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yhr127w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yhr127w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yhr127w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yhr127w-protein”, is increased cytoplasmic.

The sequence of Yhr137w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as aromatic amino acid aminotransferaseII.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “aromatic amino acid aminotransferase II” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yhr137w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yhr137w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yhr137w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yhr137w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “aromatic amino acid aminotransferase II”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “aromatic amino acid aminotransferase II”, isincreased cytoplasmic.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “aromatic amino acid aminotransferase II”, isincreased plastidic.

The sequence of Yil099w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as glucoamylase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “glucoamylase” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yil099w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yil099w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yil099w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yil099w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “glucoamylase”, preferably it is the moleculeof section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “glucoamylase”, is increased cytoplasmic.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “glucoamylase”, is increased plastidic.

The sequence of Yil147c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as histidine kinase osmosensor thatregulates an osmosensing MAP kinase cascade.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “histidine kinase osmosensor that regulates anosmosensing MAP kinase cascade” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yil147c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yil147c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yil147c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yil147c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “histidine kinase osmosensor that regulatesan osmosensing MAP kinase cascade”, preferably it is the molecule ofsection (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “histidine kinase osmosensor that regulatesan osmosensing MAP kinase cascade”, is increased cytoplasmic.

The sequence of Yir034c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as saccharopine dehydrogenase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “saccharopine dehydrogenase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yir034c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yir034c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yir034c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yir034c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “saccharopine dehydrogenase”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “saccharopine dehydrogenase”, is increasedcytoplasmic.

The sequence of Yjl013c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as spindle checkpoint complex subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “spindle checkpoint complex subunit” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl013c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl013c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl013c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl013c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “spindle checkpoint complex subunit”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “spindle checkpoint complex subunit”, isincreased cytoplasmic.

The sequence of Yjl041w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as nuclear pore complex subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “nuclear pore complex subunit” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl041w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl041w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl041w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl041w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “nuclear pore complex subunit”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “nuclear pore complex subunit”, is increasedcytoplasmic.

The sequence of Yjl064w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yjl064w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yjl064w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl064w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl064w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl064w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl064w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yjl064w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yjl064w-protein”, is increased cytoplasmic.

The sequence of Yjl067w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yjl067w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yjl067w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl067w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl067w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl067w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl067w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yjl067w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yjl067w-protein”, is increased cytoplasmic.

The sequence of Yjl094c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as potassium:hydrogen antiporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “potassium:hydrogen antiporter” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl094c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl094c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl094c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl094c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “potassium:hydrogen antiporter”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “potassium:hydrogen antiporter”, is increasedcytoplasmic.

The sequence of Yjl171c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as GPI-anchored cell wall protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “GPI-anchored cell wall protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl171c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl171c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl171c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl171c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “GPI-anchored cell wall protein”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “GPI-anchored cell wall protein”, isincreased cytoplasmic.

The sequence of Yjl213w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yjl213w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yjl213w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjl213w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjl213w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjl213w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjl213w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yjl213w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yjl213w-protein”, is increased cytoplasmic.

The sequence of Yjr017c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as peptidyl-prolyl cis-trans isomerase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “peptidyl-prolyl cis-trans isomerase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr017c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr017c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr017c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjr017c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “peptidyl-prolyl cis-trans isomerase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “peptidyl-prolyl cis-trans isomerase”, isincreased cytoplasmic.

The sequence of Yjr058c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as clathrin associated protein complexsmall subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “clathrin associated protein complex small subunit”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr058c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr058c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr058c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjr058c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “clathrin associated protein complex smallsubunit”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “clathrin associated protein complex smallsubunit”, is increased cytoplasmic.

The sequence of Yjr117w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as zinc metalloprotease.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “zinc metalloprotease” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr117w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr117w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr117w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjr117w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “zinc metalloprotease”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “zinc metalloprotease”, is increasedcytoplasmic.

The sequence of Yjr121w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as F1F0 ATP synthase beta subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “F1F0 ATP synthase beta subunit” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr121w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr121w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr121w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjr121w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “F1F0 ATP synthase beta subunit”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “F1F0 ATP synthase beta subunit”, isincreased cytoplasmic.

The sequence of Yjr131w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as alpha-mannosidase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “alpha-mannosidase” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr131w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr131w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr131w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjr131w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “alpha-mannosidase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “alpha-mannosidase”, is increasedcytoplasmic.

The sequence of Yjr145c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ribosomal protein of the smallsubunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ribosomal protein of the small subunit” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr145c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr145c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr145c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yjr145c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ribosomal protein of the small subunit”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ribosomal protein of the small subunit”, isincreased cytoplasmic.

The sequence of Ykl084w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as mitochondrial intermembrane spaceprotein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “mitochondrial intermembrane space protein” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl084w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl084w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl084w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl084w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “mitochondrial intermembrane space protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “mitochondrial intermembrane space protein”,is increased cytoplasmic.

The sequence of Ykl088w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as phosphopantothenoylcysteinedecarboxylase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “phosphopantothenoylcysteine decarboxylase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl088w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl088w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl088w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl088w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “phosphopantothenoylcysteine decarboxylase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “phosphopantothenoylcysteine decarboxylase”,is increased cytoplasmic.

The sequence of Ykl100c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ykl100c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ykl100c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl100c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl100c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl100c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl100c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ykl100c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ykl100c-protein”, is increased cytoplasmic.

The sequence of Ykl131w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ykl131w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ykl131w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl131w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl131w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl131w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl131w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ykl131w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ykl131w-protein”, is increased cytoplasmic.

The sequence of Ykl138c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as mitochondrial ribosomal protein ofthe large subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “mitochondrial ribosomal protein of the large subunit”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl138c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl138c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl138c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl138c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “mitochondrial ribosomal protein of the largesubunit”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “mitochondrial ribosomal protein of the largesubunit”, is increased cytoplasmic.

The sequence of Ykl178c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as G protein coupled pheromone receptorreceptor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “G protein coupled pheromone receptor receptor” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl178c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl178c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl178c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl178c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “G protein coupled pheromone receptorreceptor”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “G protein coupled pheromone receptorreceptor”, is increased cytoplasmic.

The sequence of Ykl179c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as golgi membrane protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “golgi membrane protein” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl179c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl179c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl179c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl179c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “golgi membrane protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “golgi membrane protein”, is increasedcytoplasmic.

The sequence of Ykl193c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as regulatory subunit of Glc7p type 1protein serine-threonine phosphatase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl193c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl193c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl193c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl193c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase”, preferably it is the molecule of section(a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase”, is increased cytoplasmic.

The sequence of Ykl216w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as dihydroorotate dehydrogenase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “dihydroorotate dehydrogenase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl216w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl216w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl216w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykl216w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “dihydroorotate dehydrogenase”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “dihydroorotate dehydrogenase”, is increasedcytoplasmic.

The sequence of Ykr016w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ykr016w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ykr016w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr016w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr016w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr016w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr016w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ykr016w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ykr016w-protein”, is increased cytoplasmic.

The sequence of Ykr021w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ykr021w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ykr021w-protein”from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr021w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr021w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr021w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr021w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ykr021w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ykr021w-protein”, is increased cytoplasmic.

The sequence of Ykr055w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “non-essential small GTPase of the Rho/Rac subfamilyof Ras-like proteins” from Saccharomyces cerevisiae or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr055w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr055w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr055w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr055w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “non-essential small GTPase of the Rho/Racsubfamily of Ras-like proteins”, preferably it is the molecule ofsection (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “non-essential small GTPase of the Rho/Racsubfamily of Ras-like proteins”, is increased cytoplasmic.

The sequence of Ykr088c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as integral membrane protein localizedto late Golgi vesicles.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “integral membrane protein localized to late Golgivesicles” from Saccharomyces cerevisiae or its functional equivalent orits homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr088c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr088c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr088c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr088c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “integral membrane protein localized to lateGolgi vesicles”, preferably it is the molecule of section (a) or (b) ofthis paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “integral membrane protein localized to lateGolgi vesicles”, is increased plastidic.

The sequence of Ykr093w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as peptide transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “peptide transporter” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr093w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr093w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr093w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr093w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “peptide transporter”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “peptide transporter”, is increasedcytoplasmic.

The sequence of Ykr099w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as transcription factor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transcription factor” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr099w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr099w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr099w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr099w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transcription factor”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transcription factor”, is increasedcytoplasmic.

The sequence of Ykr100c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as transmembrane protein with a role incell wall polymer composition.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transmembrane protein with a role in cell wallpolymer composition” from Saccharomyces cerevisiae or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykr100c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykr100c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykr100c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ykr100c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transmembrane protein with a role in cellwall polymer composition”, preferably it is the molecule of section (a)or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transmembrane protein with a role in cellwall polymer composition”, is increased cytoplasmic.

The sequence of Yll014w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yll014w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yll014w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll014w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll014w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll014w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yll014w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yll014w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yll014w-protein”, is increased cytoplasmic.

The sequence of Yll016w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as non-essential Ras guanine nucleotideexchange factor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “non-essential Ras guanine nucleotide exchange factor”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll016w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll016w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll016w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yll016w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “non-essential Ras guanine nucleotideexchange factor”, preferably it is the molecule of section (a) or (b) ofthis paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “non-essential Ras guanine nucleotideexchange factor”, is increased cytoplasmic.

The sequence of Yll023c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yll023c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yll023c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll023c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll023c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll023c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yll023c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yll023c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yll023c-protein”, is increased cytoplasmic.

The sequence of Yll037w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yll037w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yll037w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll037w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll037w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll037w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yll037w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yll037w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yll037w-protein”, is increased cytoplasmic.

The sequence of Yll049w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yll049w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yll049w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll049w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll049w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll049w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yll049w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yll049w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yll049w-protein”, is increased cytoplasmic.

The sequence of Yll055w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as cysteine transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “cysteine transporter” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll055w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll055w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll055w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yll055w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “cysteine transporter”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “cysteine transporter”, is increasedcytoplasmic.

The sequence of Ylr034c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as metal ion transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “metal ion transporter” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr034c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr034c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr034c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr034c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “metal ion transporter”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “metal ion transporter”, is increasedcytoplasmic.

The sequence of Ylr042c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ylr042c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ylr042c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr042c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr042c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr042c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr042c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ylr042c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ylr042c-protein”, is increased cytoplasmic.

The sequence of Ylr053c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YLR053c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YLR053c— protein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr053c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr053c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr053c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr053c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YLR053c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YLR053c-protein”, is increased cytoplasmic.

The sequence of Ylr058c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as cytosolic serinehydroxymethyltransferase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “cytosolic serine hydroxymethyltransferase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr058c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr058c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr058c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr058c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “cytosolic serine hydroxymethyltransferase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “cytosolic serine hydroxymethyltransferase”,is increased cytoplasmic.

The sequence of Ylr060w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as subunit of cytoplasmicphenylalanyl-tRNA synthetase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “subunit of cytoplasmic phenylalanyl-tRNA synthetase”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr060w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr060w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr060w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr060w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “subunit of cytoplasmic phenylalanyl-tRNAsynthetase”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “subunit of cytoplasmic phenylalanyl-tRNAsynthetase”, is increased cytoplasmic.

The sequence of Ylr065c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ylr065c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ylr065c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr065c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr065c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr065c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr065c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ylr065c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ylr065c-protein”, is increased cytoplasmic.

The sequence of Ylr070c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as xylitol dehydrogenase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “xylitol dehydrogenase”from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr070c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr070c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr070c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr070c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “xylitol dehydrogenase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “xylitol dehydrogenase”, is increasedcytoplasmic.

The sequence of Ylr100w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as 3-keto sterol reductase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “3-keto sterol reductase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr100w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr100w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr100w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr100w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “3-keto sterol reductase”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “3-keto sterol reductase”, is increasedcytoplasmic.

The sequence of Ylr109w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as alkyl hydroperoxide reductase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “alkyl hydroperoxide reductase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr109w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr109w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr109w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr109w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “alkyl hydroperoxide reductase”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “alkyl hydroperoxide reductase”, is increasedcytoplasmic.

The sequence of Ylr125w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ylr125w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ylr125w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr125w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr125w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr125w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr125w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ylr125w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ylr125w-protein”, is increased cytoplasmic.

The sequence of Ylr127c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as anaphase promoting complex (APC)subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “anaphase promoting complex (APC) subunit” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr127c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr127c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr127c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr127c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “anaphase promoting complex (APC) subunit”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “anaphase promoting complex (APC) subunit”,is increased cytoplasmic.

The sequence of Ylr185w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as protein component of the largeribosomal subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein component of the large ribosomal subunit”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr185w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr185w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr185w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr185w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein component of the large ribosomalsubunit”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein component of the large ribosomalsubunit”, is increased cytoplasmic.

The sequence of Ylr204w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as mitochondrial protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “mitochondrial protein” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr204w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr204w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr204w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr204w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “mitochondrial protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “mitochondrial protein”, is increasedcytoplasmic.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “mitochondrial protein”, is increasedplastidic.

The sequence of Ylr242c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ARV1 protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ARV1 protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr242c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr242c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr242c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr242c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ARV1 protein”, preferably it is the moleculeof section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ARV1 protein”, is increased cytoplasmic.

The sequence of Ylr293c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as GTP-binding protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “GTP-binding protein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr293c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr293c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr293c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr293c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “GTP-binding protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “GTP-binding protein”, is increasedcytoplasmic.

The sequence of Ylr313c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as protein involved in shmoo formationand bipolar bud site selection.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein involved in shmoo formation and bipolar budsite selection” from Saccharomyces cerevisiae or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr313c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr313c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr313c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr313c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein involved in shmoo formation andbipolar bud site selection”, preferably it is the molecule of section(a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein involved in shmoo formation andbipolar bud site selection”, is increased cytoplasmic.

The sequence of Ylr315w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as non-essential kinetochore protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “non-essential kinetochore protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr315w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr315w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr315w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr315w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “non-essential kinetochore protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “non-essential kinetochore protein”, isincreased cytoplasmic.

The sequence of Ylr329w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Meiotic recombination protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Meiotic recombination protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr329w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr329w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr329w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr329w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Meiotic recombination protein”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Meiotic recombination protein”, is increasedcytoplasmic.

The sequence of Ylr362w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as signal transducing MEK kinase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “signal transducing MEK kinase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr362w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr362w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr362w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr362w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “signal transducing MEK kinase”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “signal transducing MEK kinase”, is increasedcytoplasmic.

The sequence of Ylr395c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as cytochrome c oxidase subunit VIII.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “cytochrome c oxidase subunit VIII” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr395c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr395c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr395c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr395c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “cytochrome c oxidase subunit VIII”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “cytochrome c oxidase subunit VIII”, isincreased cytoplasmic.

The sequence of Ylr404w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ylr404w-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ylr404w-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr404w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr404w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr404w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr404w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ylr404w-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ylr404w-protein”, is increased cytoplasmic.

The sequence of Ylr463c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ylr463c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ylr463c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr463c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr463c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr463c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ylr463c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ylr463c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ylr463c-protein”, is increased cytoplasmic.

The sequence of Yml022w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as adenine phosphoribosyltransferase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “adenine phosphoribosyltransferase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yml022w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yml022w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yml022w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yml022w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “adenine phosphoribosyltransferase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “adenine phosphoribosyltransferase”, isincreased cytoplasmic.

The sequence of Yml027w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Mcm1p binding transcriptionalrepressor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Mcm1p binding transcriptional repressor” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yml027w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yml027w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yml027w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yml027w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Mcm1p binding transcriptional repressor”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Mcm1p binding transcriptional repressor”, isincreased cytoplasmic.

The sequence of Yml065w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as origin recognition complex subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “origin recognition complex subunit” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yml065w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yml065w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yml065w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yml065w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “origin recognition complex subunit”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “origin recognition complex subunit”, isincreased cytoplasmic.

The sequence of Yml089c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yml089c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yml089c-protein”from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yml089c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yml089c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yml089c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yml089c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yml089c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yml089c-protein”, is increased cytoplasmic.

The sequence of Yml128c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as yml128c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “yml128c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yml128c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yml128c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yml128c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yml128c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “yml128c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “yml128c-protein”, is increased cytoplasmic.

The sequence of Ymr011w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as hexose transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “hexose transporter” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr011w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr011w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr011w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr011w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “hexose transporter”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “hexose transporter”, is increasedcytoplasmic.

The sequence of Ymr037c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Zinc finger protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Zinc finger protein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr037c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr037c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr037c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr037c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Zinc finger protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Zinc finger protein”, is increasedcytoplasmic.

The sequence of Ymr049c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as protein required for maturation ofribosomal RNAs.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein required for maturation of ribosomal RNAs”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr049c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr049c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr049c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr049c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein required for maturation of ribosomalRNAs”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein required for maturation of ribosomalRNAs”, is increased cytoplasmic.

The sequence of Ymr052w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Factor arrest protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Factor arrest protein” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr052w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr052w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr052w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr052w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Factor arrest protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Factor arrest protein”, is increasedcytoplasmic.

The sequence of Ymr082c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YMR082C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR082c— protein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr082c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr082c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr082c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr082c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR082C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR082C-protein”, is increased cytoplasmic.

The sequence of YMR125W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Nuclear cap-binding protein complexsubunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Nuclear cap-binding protein complex subunit” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YMR125W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YMR125W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YMR125W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YMR125W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Nuclear cap-binding protein complexsubunit”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Nuclear cap-binding protein complexsubunit”, is increased cytoplasmic.

The sequence of Ymr126c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YMR126c membrane protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR126c membrane protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr126c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr126c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr126c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr126c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR126c membrane protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR126c membrane protein”, is increasedcytoplasmic.

The sequence of Ymr144w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YMR144W-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR144W-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr144w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr144w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr144w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr144w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR144W-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR144W-protein”, is increased cytoplasmic.

The sequence of Ymr160w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YMR160W-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR160W-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr160w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr160w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, and being depicted in the same    respective line as said Ymr160w or a functional equivalent or a    homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said Ymr160w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR160W-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR160W-protein”, is increased cytoplasmic.

The sequence of Ymr191w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Stationary phase protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Stationary phase protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr191w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr191w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr191w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr191w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Stationary phase protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Stationary phase protein”, is increasedcytoplasmic.

The sequence of Ymr209c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YMR209C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR209C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr209c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr209c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr209c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr209c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR209C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR209C-protein”, is increased cytoplasmic.

The sequence of Ymr233w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YMR233W-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR233W-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr233w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr233w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr233w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr233w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR233W-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR233W-protein”, is increased cytoplasmic.

The sequence of Ymr278w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described asphosphoglucomutase/phosphomannomutase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “phosphoglucomutase/phosphomannomutase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr278w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr278w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr278w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr278w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “phosphoglucomutase/phosphomannomutase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “phosphoglucomutase/phosphomannomutase”, isincreased cytoplasmic.

The sequence of Ymr280c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Regulatory CAT8 protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Regulatory CAT8 protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr280c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr280c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr280c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ymr280c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Regulatory CAT8 protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Regulatory CAT8 protein”, is increasedcytoplasmic.

The sequence of Ynl014w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as translational elongation factor EF-3(HEF3).

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “translational elongation factor EF-3 (HEF3)” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ynl014w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ynl014w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ynl014w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ynl014w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “translational elongation factor EF-3(HEF3)”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “translational elongation factor EF-3(HEF3)”, is increased cytoplasmic.

The sequence of Ynl320w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YNL320W-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YNL320W-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ynl320w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ynl320w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ynl320w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ynl320w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YNL320W-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YNL320W-protein”, is increased cytoplasmic.

The sequence of Yol007c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Chitin synthase 3 complex protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Chitin synthase 3 complex protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yol007c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yol007c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yol007c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yol007c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Chitin synthase 3 complex protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Chitin synthase 3 complex protein”, isincreased cytoplasmic.

The sequence of Yol164w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Alkyl/aryl-sulfatase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Alkyl/aryl-sulfatase” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yol164w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yol164w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yol164w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yol164w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Alkyl/aryl-sulfatase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Alkyl/aryl-sulfatase”, is increasedcytoplasmic.

The sequence of Yor076c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as antiviral adaptor protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “antiviral adaptor protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yor076c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yor076c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yor076c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yor076c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “antiviral adaptor protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “antiviral adaptor protein”, is increasedcytoplasmic.

The sequence of Yor083w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as repressor of G1 transcription.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “repressor of G1 transcription” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yor083w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yor083w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yor083w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yor083w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “repressor of G1 transcription”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “repressor of G1 transcription”, is increasedcytoplasmic.

The sequence of Yor097c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YOR097c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YOR097c— protein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yor097c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yor097c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yor097c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yor097c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YOR097c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YOR097c-protein”, is increased cytoplasmic.

The sequence of Yor128c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Phosphoribosylaminoimidazolecarboxylase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Phosphoribosylaminoimidazole carboxylase” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yor128c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yor128c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yor128c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yor128c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Phosphoribosylaminoimidazole carboxylase”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Phosphoribosylaminoimidazole carboxylase”,is increased cytoplasmic.

The sequence of Yor353c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as component of the RAM signalingnetwork.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “component of the RAM signaling network” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yor353c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yor353c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yor353c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Yor353c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “component of the RAM signaling network”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “component of the RAM signaling network”, isincreased cytoplasmic.

The sequence of Ypl141c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as protein kinase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein kinase” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ypl141c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ypl141c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ypl141c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ypl141c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein kinase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein kinase”, is increased cytoplasmic.

The sequence of Ypr088c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as signal recognition particle subunit(SRP54).

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “signal recognition particle subunit (SRP54)” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ypr088c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ypr088c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, and being depicted in the same    respective line as said Ypr088c or a functional equivalent or a    homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said Ypr088c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “signal recognition particle subunit(SRP54)”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “signal recognition particle subunit(SRP54)”, is increased cytoplasmic.

The sequence of Ypr108w from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as regulatory subunit of the 26Sproteasome.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “regulatory subunit of the 26S proteasome” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ypr108w or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ypr108w; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ypr108w or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ypr108w,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “regulatory subunit of the 26S proteasome”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “regulatory subunit of the 26S proteasome”,is increased cytoplasmic.

The sequence of Ypr110c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as RNA polymerase III subunit.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “RNA polymerase III subunit” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ypr110c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ypr110c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ypr110c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said Ypr110c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “RNA polymerase III subunit”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “RNA polymerase III subunit”, is increasedcytoplasmic.

The sequence of B3825_(—)2 from Escherichia coli, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as lysophospholipase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “lysophospholipase” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3825_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said B3825_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3825_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said B3825_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “lysophospholipase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “lysophospholipase”, is increased plastidic.

The sequence of Yir034c_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as saccharopine dehydrogenase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “saccharopine dehydrogenase” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yir034c_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yir034c_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yir034c_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Yir034c_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “saccharopine dehydrogenase”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “saccharopine dehydrogenase”, is increasedcytoplasmic.

The sequence of Yjr131w_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as alpha-mannosidase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “alpha-mannosidase” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yjr131w_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yjr131w_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yjr131w_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Yjr131w_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “alpha-mannosidase”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “alpha-mannosidase”, is increasedcytoplasmic.

The sequence of Ykl100c_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as ykl100c-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ykl100c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl100c_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl100c_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl100c_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Ykl100c_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ykl100c-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ykl100c-protein”, is increased cytoplasmic.

The sequence of Ykl193c_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as regulatory subunit of Glc7ptype 1 protein serine-threonine phosphatase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ykl193c_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ykl193c_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ykl193c_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Ykl193c_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase”, preferably it is the molecule of section(a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase”, is increased cytoplasmic.

The sequence of Yll016w_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as non-essential Ras guaninenucleotide exchange factor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “non-essential Ras guanine nucleotide exchange factor”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Yll016w_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Yll016w_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Yll016w_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Yll016w_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “non-essential Ras guanine nucleotideexchange factor”, preferably it is the molecule of section (a) or (b) ofthis paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “non-essential Ras guanine nucleotideexchange factor”, is increased cytoplasmic.

The sequence of Ylr034c_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as metal ion transporter.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “metal ion transporter” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr034c_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr034c_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr034c_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Ylr034c_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “metal ion transporter”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “metal ion transporter”, is increasedcytoplasmic.

The sequence of Ylr060w_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as subunit of cytoplasmicphenylalanyl-tRNA synthetase.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “subunit of cytoplasmic phenylalanyl-tRNA synthetase”from Saccharomyces cerevisiae or its functional equivalent or itshomolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ylr060w_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ylr060w_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ylr060w_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Ylr060w_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “subunit of cytoplasmic phenylalanyl-tRNAsynthetase”, preferably it is the molecule of section (a) or (b) of thisparagraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “subunit of cytoplasmic phenylalanyl-tRNAsynthetase”, is increased cytoplasmic.

The sequence of YMR082C_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as YMR082C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YMR082c-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YMR082C_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YMR082C_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YMR082C_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said YMR082C_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YMR082C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YMR082C-protein”, is increased cytoplasmic.

The sequence of B1258 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as B1258-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “B1258-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1258 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1258; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1258 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1258,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “B1258-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “B1258-protein”, is increased cytoplasmic.

The sequence of YML101C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YML101C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YML101C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YML101C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YML101C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YML101C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YML101C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YML101C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YML101C-protein”, is increased cytoplasmic.

The sequence of YMR065W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as nuclear fusion protein precursor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “nuclear fusion protein precursor” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YMR065W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YMR065W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YMR065W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YMR065W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “nuclear fusion protein precursor”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “nuclear fusion protein precursor”, isincreased cytoplasmic.

The sequence of YMR163c from Saccharomyces cerevisiae, e.g. as shown incolumn of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as inheritance of peroxisomes protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “inheritance of peroxisomes protein” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YMR163c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YMR163c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YMR163c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YMR163c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “inheritance of peroxisomes protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “inheritance of peroxisomes protein”, isincreased cytoplasmic.

The sequence of YOL042W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as exoribonuclease.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “exoribonuclease” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YOL042W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YOL042W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YOL042W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YOL042W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “exoribonuclease”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “exoribonuclease”, is increased cytoplasmic.

The sequence of YOR226c from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as iron sulfur cluster assemblyprotein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “iron sulfur cluster assembly protein” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YOR226c or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YOR226c; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YOR226c or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YOR226c,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “iron sulfur cluster assembly protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “iron sulfur cluster assembly protein”, isincreased cytoplasmic.

The sequence of YPL068C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YPL068C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YPL068C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YPL068C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YPL068C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YPL068C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YPL068C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YPL068C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YPL068C-protein”, is increased cytoplasmic.

The sequence of B0165 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as B0165-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “B0165-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B0165 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B0165; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B0165 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B0165,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “B0165-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “60165-protein”, is increased plastidic.

The sequence of YOR203W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YOR203W-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YOR203W-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YOR203W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YOR203W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YOR203W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YOR203W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YOR203W-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YOR203W-protein”, is increased cytoplasmic.

The sequence of YNL147W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as ribonucleoprotein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “ribonucleoprotein” from Saccharomyces cerevisiae orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YNL147W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YNL147W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YNL147W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YNL147W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “ribonucleoprotein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “ribonucleoprotein”, is increasedcytoplasmic.

The sequence of YBR083W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as transcription factor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transcription factor” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YBR083W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YBR083W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YBR083W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YBR083W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transcription factor”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transcription factor”, is increasedcytoplasmic.

The sequence of YKL111C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YKL111C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YKL111C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YKL111C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YKL111C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YKL111C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YKL111C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YKL111C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YKL111C-protein”, is increased cytoplasmic.

The sequence of YPR067W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as iron sulfur cluster assemblyprotein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “iron sulfur cluster assembly protein” fromSaccharomyces cerevisiae or its functional equivalent or its homolog,e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YPR067W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YPR067W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YPR067W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YPR067W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “iron sulfur cluster assembly protein”,preferably it is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “iron sulfur cluster assembly protein”, isincreased cytoplasmic.

The sequence of B1985 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as transport protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transport protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1985 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1985; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1985 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1985,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transport protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transport protein”, is increasedcytoplasmic.

The sequence of B3838 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as protein translocase protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “protein translocase protein” from Escherichia coli orits functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B3838 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B3838; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B3838 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B3838,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “protein translocase protein”, preferably itis the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “protein translocase protein”, is increasedcytoplasmic.

The sequence of YJL010C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YJL010C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YJL010C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YJL010C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YJL010C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YJL010C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YJL010C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YJL010C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YJL010C-protein”, is increased cytoplasmic.

The sequence of B1267 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as B1267-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “B1267-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1267 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1267; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1267 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1267,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “B1267-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “B1267-protein”, is increased cytoplasmic.

The sequence of B1322 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as membrane protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “membrane protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1322 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1322; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1322 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1322,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “membrane protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “membrane protein”, is increased cytoplasmic.

The sequence of B1381 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as B1381-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “61381-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B1381 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B1381; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B1381 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B1381,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “B1381-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “B1381-protein”, is increased cytoplasmic.

The sequence of B2646 from Escherichia coli, e.g. as shown in column 5of table I, application no. 1, is published (e.g. sequences fromSaccharomyces cerevisiae have been published in Goffeau et al., Science274 (5287), 546 (1996), sequences from Escherichia coli have beenpublished in Blattner et al., Science 277 (5331), 1453 (1997)), and/orits activity is described as B2646-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “B2646-protein” from Escherichia coli or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said B2646 or a functional equivalent    or a homologue thereof as shown in column 7 of table I, application    no. 1, preferably a homologue or functional equivalent as shown in    column 7 of table I B, application no. 1, and being depicted in the    same respective line as said B2646; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said B2646 or a functional equivalent or    a homologue thereof as depicted in column 7 of table II, application    no. 1, preferably a homologue or functional equivalent as depicted    in column 7 of table II B, application no. 1, and being depicted in    the same respective line as said B2646,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “B2646-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “B2646-protein”, is increased cytoplasmic.

The sequence of YBR191W from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as 60S ribosomal protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “60S ribosomal protein” from Saccharomyces cerevisiaeor its functional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YBR191W or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YBR191W; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YBR191W or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YBR191W,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “60S ribosomal protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “60S ribosomal protein”, is increasedcytoplasmic.

The sequence of YDL135C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as Rho GDP-dissociation inhibitor.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Rho GDP-dissociation inhibitor” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YDL135C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YDL135C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YDL135C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YDL135C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Rho GDP-dissociation inhibitor”, preferablyit is the molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Rho GDP-dissociation inhibitor”, isincreased cytoplasmic.

The sequence of YHL005C from Saccharomyces cerevisiae, e.g. as shown incolumn 5 of table I, application no. 1, is published (e.g. sequencesfrom Saccharomyces cerevisiae have been published in Goffeau et al.,Science 274 (5287), 546 (1996), sequences from Escherichia coli havebeen published in Blattner et al., Science 277 (5331), 1453 (1997)),and/or its activity is described as YHL005C-protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “YHL005C-protein” from Saccharomyces cerevisiae or itsfunctional equivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YHL005C or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YHL005C; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YHL005C or a functional equivalent    or a homologue thereof as depicted in column 7 of table II,    application no. 1, preferably a homologue or functional equivalent    as depicted in column 7 of table II B, application no. 1, and being    depicted in the same respective line as said YHL005C,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “YHL005C-protein”, preferably it is themolecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “YHL005C-protein”, is increased cytoplasmic.

The sequence of YKR100C_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as transmembrane protein witha role in cell wall polymer composition.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “transmembrane protein with a role in cell wallpolymer composition” from Saccharomyces cerevisiae or its functionalequivalent or its homolog, e.g. the increase of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said YKR100C_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said YKR100C_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said YKR100C_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said YKR100C_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “transmembrane protein with a role in cellwall polymer composition”, preferably it is the molecule of section (a)or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “transmembrane protein with a role in cellwall polymer composition”, is increased cytoplasmic.

The sequence of Ymr191w_(—)2 from Saccharomyces cerevisiae, e.g. asshown in column 5 of table I, application no. 1, is published (e.g.sequences from Saccharomyces cerevisiae have been published in Goffeauet al., Science 274 (5287), 546 (1996), sequences from Escherichia colihave been published in Blattner et al., Science 277 (5331), 1453(1997)), and/or its activity is described as Stationary phase protein.

Accordingly, in one embodiment, the process of the present inventioncomprises increasing or generating the activity of a gene product withthe activity of a “Stationary phase protein” from Saccharomycescerevisiae or its functional equivalent or its homolog, e.g. theincrease of

-   (a) a gene product of a gene comprising the nucleic acid molecule as    shown in column 5 of table I, application no. 1, and being depicted    in the same respective line as said Ymr191w_(—)2 or a functional    equivalent or a homologue thereof as shown in column 7 of table I,    application no. 1, preferably a homologue or functional equivalent    as shown in column 7 of table I B, application no. 1, and being    depicted in the same respective line as said Ymr191w_(—)2; or-   (b) a polypeptide comprising a polypeptide, a consensus sequence or    a polypeptide motif as shown in column 5 of table II or in column 7    of table IV, application no. 1, respectively, and being depicted in    the same respective line as said Ymr191w_(—)2 or a functional    equivalent or a homologue thereof as depicted in column 7 of table    II, application no. 1, preferably a homologue or functional    equivalent as depicted in column 7 of table II B, application no. 1,    and being depicted in the same respective line as said Ymr191w_(—)2,    as mentioned herein, for an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, plant or part    thereof in plant cell, plant or part thereof, as mentioned,    especially for an enhanced NUE, or increased biomass production, or    an enhanced NUE and increased biomass production.

Accordingly, in one embodiment, the molecule which activity is to beincreased in the process of the invention is the gene product with anactivity of described as a “Stationary phase protein”, preferably it isthe molecule of section (a) or (b) of this paragraph.

In one embodiment, said molecule, which activity is to be increased inthe process of the invention and which is the gene product with anactivity as described as a “Stationary phase protein”, is increasedcytoplasmic.

Surprisingly, it was observed that an increasing or generating of atleast one gene conferring an activity selected from the group consistingof 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease or of a gene comprising anucleic acid sequence described in column 5 of table I, application no.1, in a plant conferred an increased yield, especially an enhanced NUEand/or increased biomass production, in the transformed plants ascompared to a corresponding non-transformed wild type plant, especiallyan enhanced NUE, or an increased biomass production, or an enhanced NUEand increased biomass production.

Surprisingly, it was observed that an increasing or generating of atleast one gene conferring an activity selected from the group consistingof 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol reductase,60S ribosomal protein, adenine phosphoribosyltransferase, adenylatekinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease or of a gene comprising anucleic acid sequence described in column 5 of table I, application no.1, in Arabidopsis thaliana conferred an increased yield, especially anenhanced NUE and/or increased biomass production in the transformedplants as compared to a corresponding non-transformed wild type plant,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and increased biomass production.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b0017-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 38 ora nucleic acid which differs from the nucleic acid SEQ ID NO. 38 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased yield, especially an increased NUE than the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “b0017-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 38 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 38 by exchanging the stopcodon taa by tga in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b0017-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 38 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 38 by exchanging the stopcodon taa by tga in Arabidopsis thaliana conferred an increased NUE andan increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transport protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 42 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transport protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 42 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transport protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 42 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “hydroxymyristol acylcarrier protein dehydratase” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 123 or a nucleic acid which differs from thenucleic acid SEQ ID NO. 123 by exchanging the stop codon taa by tga inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hydroxymyristol acyl carrierprotein dehydratase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 123 or a nucleic acid which differs from thenucleic acid SEQ ID NO. 123 by exchanging the stop codon taa by tga inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hydroxymyristol acyl carrierprotein dehydratase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 123 or a nucleic acid which differs from the nucleicacid SEQ ID NO. 123 by exchanging the stop codon taa by tga inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “gamma-glutamylkinase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 380 in Arabidopsis thaliana conferred an increased yield, especiallyan increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “gamma-glutamyl kinase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 380 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “gamma-glutamyl kinase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 380 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “alpha-glucosidase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 679 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alpha-glucosidase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 679 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alpha-glucosidase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 679 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “adenylate kinase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 812 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “adenylate kinase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 812 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “adenylate kinase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 812 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a“2-dehydro-3-deoxy-phosphoheptonate aldolase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 1055 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “2-dehydro-3-deoxy-phosphoheptonatealdolase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 1055 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “2-dehydro-3-deoxy-phosphoheptonatealdolase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 1055 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “molybdopterinbiosynthesis protein” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 1563 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “molybdopterin biosynthesis protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 1563in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “molybdopterin biosynthesis protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 1563in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “hydroxylaminereductase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 1705 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hydroxylamine reductase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO.: 1705 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hydroxylamine reductase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 1705 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “prolinedehydrogenase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 1844 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “proline dehydrogenase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 1844 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “proline dehydrogenase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 1844 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “PhoH-like protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 1950in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “PhoH-like protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 1950 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “PhoH-like protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 1950 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “isomerase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 1975 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “isomerase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 1975 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “isomerase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 1975 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b1933-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2127or a nucleic acid which differs from the nucleic acid SEQ

ID NO. 2127 by exchanging the stop codon taa by tga in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b1933-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 2127 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 2127 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b1933-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 2127 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 2127 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increased NUEand an increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “glycosyltransferase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2135or a nucleic acid which differs from the nucleic acid SEQ ID NO. 2135 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glycosyltransferase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 2135 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 2135 by exchangingthe stop codon taa by tga in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glycosyltransferase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 2135 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 2135 by exchangingthe stop codon taa by tga in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b2165-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2171in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2165-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 2171 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2165-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 2171 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “short chain fattyacid transporter” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 2297 or a nucleic acid which differs from the nucleic acidSEQ ID NO. 2297 by exchanging the stop codon taa by tga in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “short chain fatty acid transporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 2297or a nucleic acid which differs from the nucleic acid SEQ ID NO. 2297 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “short chain fatty acid transporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2297or a nucleic acid which differs from the nucleic acid SEQ ID NO. 2297 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b2238-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2426or a nucleic acid which differs from the nucleic acid SEQ ID NO. 2426 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2238-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 2426 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 2426 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2238-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 2426 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 2426 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increased NUEand an increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a“lysine/arginine/ornithine transporter subunit” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 2452 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 2452 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysine/arginine/ornithinetransporter subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 2452 or a nucleic acid which differs from thenucleic acid SEQ ID NO. 2452 by exchanging the stop codon taa by tga inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysine/arginine/ornithinetransporter subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 2452 or a nucleic acid which differs from thenucleic acid SEQ ID NO. 2452 by exchanging the stop codon taa by tga inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b2431-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2551in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2431-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 2551 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2431-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 2551 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “chorismate mutaseT/prephenate dehydrogenase (bifunctional)” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 2600 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “chorismate mutase T/prephenatedehydrogenase (bifunctional)” encoded by a gene comprising the nucleicacid sequence SEQ ID NO.: 2600 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “chorismate mutase T/prephenatedehydrogenase (bifunctional)” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 2600 in Arabidopsis thaliana conferred anincreased NUE and an increased biomass production compared with the wildtype control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b2766-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 2668in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2766-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 2668 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b2766-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 2668 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “glycinedecarboxylase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 2772 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glycine decarboxylase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 2772 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glycine decarboxylase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 2772 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “threonineammonia-lyase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 3117 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “threonine ammonia-lyase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO.: 3117 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “threonine ammonia-lyase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 3117 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “b3120-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 3390or a nucleic acid which differs from the nucleic acid SEQ ID NO. 3390 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b3120-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 3390 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 3390 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “b3120-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 3390 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 3390 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increased NUEand an increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “outer membrane usherprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 3396 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “outer membrane usher protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 3396in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “outer membrane usher protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 3396in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “glycerol-3-phosphatetransporter subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 3470 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glycerol-3-phosphate transportersubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 3470 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glycerol-3-phosphate transportersubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 3470 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “hydro-lyase” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 3563 or anucleic acid which differs from the nucleic acid SEQ ID NO. 3563 byexchanging the stop codon taa by tga in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hydro-lyase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 3563 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 3563 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hydro-lyase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 3563 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 3563 by exchanging thestop codon taa by tga in Arabidopsis thaliana conferred an increased NUEand an increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “lysophospholipase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 3770in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysophospholipase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 3770 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysophospholipase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 3770 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yal019w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 3868in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yal019w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 3868 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yal019w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 3868 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “carnitineacetyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 3895 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “carnitine acetyltransferase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 3895in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “carnitine acetyltransferase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 3895in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Transcriptionalactivator” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 3953 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Transcriptional activator” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 3953 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Transcriptional activator” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 3953 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “splicing factor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4111in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “splicing factor” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4111 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “splicing factor” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4111 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “autophagy-specificphosphatidylinositol 3-kinase complex protein subunit” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4149 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “autophagy-specificphosphatidylinositol 3-kinase complex protein subunit” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4149 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “autophagy-specificphosphatidylinositol 3-kinase complex protein subunit” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4149 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “microsomalbeta-keto-reductase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 4162 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “microsomal beta-keto-reductase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 4162in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “microsomal beta-keto-reductase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4162in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a“UDP-N-acetyl-glucosamine-1-P transferase” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 4235 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “UDP-N-acetyl-glucosamine-1-Ptransferase” encoded by a gene comprising the nucleic acid sequence SEQID NO.: 4235 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “UDP-N-acetyl-glucosamine-1-Ptransferase” encoded by a gene comprising the nucleic acid sequence SEQID NO. 4235 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ybr262c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4280in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ybr262c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4280 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ybr262c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4280 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein necessary forstructural stability of L-A double-stranded RNA-containing particles”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4288in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein necessary for structuralstability of L-A double-stranded RNA-containing particles” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 4288 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein necessary for structuralstability of L-A double-stranded RNA-containing particles” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 4288 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YDR070C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4315in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YDR070C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4315 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YDR070C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4315 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “chaperone” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 4325 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “chaperone” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4325 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “chaperone” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4325 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “helix-loop-helixtranscription activator that binds inositol/choline-responsive elements”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4335in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “helix-loop-helix transcriptionactivator that binds inositol/choline-responsive elements” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 4335 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “helix-loop-helix transcriptionactivator that binds inositol/choline-responsive elements” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 4335 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “golgi membraneexchange factor subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 4346 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “golgi membrane exchange factorsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 4346 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “golgi membrane exchange factorsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 4346 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “dihydrosphingosinephosphate lyase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 4361 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “dihydrosphingosine phosphate lyase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 4361in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “dihydrosphingosine phosphate lyase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4361in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ubiquitin regulatoryprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 4402 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ubiquitin regulatory protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 4402in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ubiquitin regulatory protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4402in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ydr355c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4431in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ydr355c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4431 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ydr355c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4431 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “lysine-specificmetalloprotease” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 4435 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysine-specific metalloprotease”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 4435in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysine-specific metalloprotease”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4435in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 4485 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “subunit of the transport proteinparticle (TRAPP) complex of the cis-Golgi” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO.: 4485 in Arabidopsis thalianaconferred an increased biomass production compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “subunit of the transport proteinparticle (TRAPP) complex of the cis-Golgi” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 4485 in Arabidopsis thalianaconferred an increased NUE and an increased biomass production comparedwith the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “myo-inositoltransporter” encoded by a gene comprising the nucleic acid sequence SEQID NO. 4506 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “myo-inositol transporter” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 4506 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “myo-inositol transporter” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 4506 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “SM complex B proteinfor mRNA splicing” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 4790 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “SM complex B protein for mRNAsplicing” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 4790 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “SM complex B protein for mRNAsplicing” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 4790 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YFR007W-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4806in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YFR007W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4806 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YFR007W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4806 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “oxidoreductase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 4836in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “oxidoreductase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 4836 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “oxidoreductase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 4836 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transcriptionelongation factor” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5311 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transcription elongation factor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 5311in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transcription elongation factor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5311in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “cytosolic catalase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5346in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cytosolic catalase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 5346 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cytosolic catalase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 5346 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ygr122c-a-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5533in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ygr122c-a-protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 5533 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ygr122c-a-protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 5533 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “v-SNARE bindingprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 5551 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “v-SNARE binding protein” encoded bya gene comprising the nucleic acid sequence SEQ ID NO.: 5551 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “v-SNARE binding protein” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 5551 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein involved insphingolipid biosynthesis” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5559 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein involved in sphingolipidbiosynthesis” encoded by a gene comprising the nucleic acid sequence SEQID NO.: 5559 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein involved in sphingolipidbiosynthesis” encoded by a gene comprising the nucleic acid sequence SEQID NO. 5559 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “mitochondrialribosomal protein of the small subunit” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 5602 in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial ribosomal protein ofthe small subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 5602 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial ribosomal protein ofthe small subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5602 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “phosphatidylserinedecarboxylase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 5608 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “phosphatidylserine decarboxylase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 5608in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “phosphatidylserine decarboxylase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5608in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “cholinephosphatecytidylyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5614 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cholinephosphatecytidylyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 5614 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cholinephosphatecytidylyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5614 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ygr266w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5666in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ygr266w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 5666 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ygr266w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 5666 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “cell wallendo-beta-1,3-glucanase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5701 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cell wall endo-beta-1,3-glucanase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 5701in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cell wall endo-beta-1,3-glucanase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5701in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ygr290w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5750in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ygr290w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 5750 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ygr290w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 5750 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yhl021c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5754in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yhl021c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 5754 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yhl021c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 5754 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “v-SNARE proteininvolved in Golgi transport” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 5778 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “v-SNARE protein involved in Golgitransport” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 5778 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “v-SNARE protein involved in Golgitransport” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 5778 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “mitochondrialseryl-tRNA synthetase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5812 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial seryl-tRNAsynthetase” encoded by a gene comprising the nucleic acid sequence SEQID NO.: 5812 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial seryl-tRNAsynthetase” encoded by a gene comprising the nucleic acid sequence SEQID NO. 5812 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yhr127w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 5967in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yhr127w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 5967 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yhr127w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 5967 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “aromatic amino acidaminotransferase II” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5973 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “aromatic amino acidaminotransferase II” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 5973 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “aromatic amino acidaminotransferase II” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 5973 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “glucoamylase” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 6027 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glucoamylase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 6027 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “glucoamylase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 6027 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “histidine kinaseosmosensor that regulates an osmosensing MAP kinase cascade” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 6107 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “histidine kinase osmosensor thatregulates an osmosensing MAP kinase cascade” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 6107 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “histidine kinase osmosensor thatregulates an osmosensing MAP kinase cascade” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 6107 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “saccharopinedehydrogenase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 6150 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “saccharopine dehydrogenase” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 6150 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “saccharopine dehydrogenase” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 6150 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “spindle checkpointcomplex subunit” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 6198 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “spindle checkpoint complex subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 6198in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “spindle checkpoint complex subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6198in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “nuclear pore complexsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 6208 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “nuclear pore complex subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 6208in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “nuclear pore complex subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6208in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yjl064w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6242in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yjl064w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 6242 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yjl064w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 6242 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yjl067w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6246in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yjl067w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 6246 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yjl067w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 6246 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “potassium:hydrogenantiporter” encoded by a gene comprising the nucleic acid sequence SEQID NO. 6250 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “potassium:hydrogen antiporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 6250in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “potassium:hydrogen antiporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6250in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “GPI-anchored cellwall protein” encoded by a gene comprising the nucleic acid sequence SEQID NO. 6297 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “GPI-anchored cell wall protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 6297in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “GPI-anchored cell wall protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6297in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yjl213w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6326in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yjl213w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 6326 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yjl213w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 6326 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “peptidyl-prolylcis-trans isomerase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 6488 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “peptidyl-prolyl cis-transisomerase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 6488 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “peptidyl-prolyl cis-transisomerase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 6488 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “clathrin associatedprotein complex small subunit” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 6550 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “clathrin associated protein complexsmall subunit” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO.: 6550 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “clathrin associated protein complexsmall subunit” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 6550 in Arabidopsis thaliana conferred an increased NUE andan increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “zinc metalloprotease”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6700in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “zinc metalloprotease” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 6700 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “zinc metalloprotease” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 6700 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “F1F0 ATP synthasebeta subunit” encoded by a gene comprising the nucleic acid sequence SEQID NO. 6816 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “F1F0 ATP synthase beta subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 6816in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “F1F0 ATP synthase beta subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 6816in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “alpha-mannosidase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 7366in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alpha-mannosidase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 7366 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alpha-mannosidase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 7366 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ribosomal protein ofthe small subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 7475 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ribosomal protein of the smallsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 7475 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ribosomal protein of the smallsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 7475 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “mitochondrialintermembrane space protein” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 7602 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial intermembrane spaceprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 7602 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial intermembrane spaceprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 7602 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a“phosphopantothenoylcysteine decarboxylase” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 7651 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “phosphopantothenoylcysteinedecarboxylase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO.: 7651 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “phosphopantothenoylcysteinedecarboxylase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 7651 in Arabidopsis thaliana conferred an increased NUE andan increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ykl100c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 7661in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykl100c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 7661 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykl100c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 7661 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ykl131w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 7675in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykl131w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 7675 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykl131w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 7675 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “mitochondrialribosomal protein of the large subunit” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 7679 in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial ribosomal protein ofthe large subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 7679 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial ribosomal protein ofthe large subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 7679 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “G protein coupledpheromone receptor receptor” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 7710 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “G protein coupled pheromonereceptor receptor” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 7710 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “G protein coupled pheromonereceptor receptor” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 7710 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “golgi membraneprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 7735 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “golgi membrane protein” encoded bya gene comprising the nucleic acid sequence SEQ ID NO.: 7735 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “golgi membrane protein” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 7735 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “regulatory subunit ofGlc7p type 1 protein serine-threonine phosphatase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 7778 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “regulatory subunit of Glc7p type 1protein serine-threonine phosphatase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO.: 7778 in Arabidopsis thaliana conferredan increased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “regulatory subunit of Glc7p type 1protein serine-threonine phosphatase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 7778 in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “dihydroorotatedehydrogenase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 7829 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “dihydroorotate dehydrogenase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 7829in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “dihydroorotate dehydrogenase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 7829in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ykr016w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8017in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykr016w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8017 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykr016w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8017 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ykr021w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8045in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykr021w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8045 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykr021w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8045 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “non-essential smallGTPase of the Rho/Rac subfamily of Ras-like proteins” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8073 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins” encoded by a gene comprising thenucleic acid sequence SEQ ID NO.: 8073 in Arabidopsis thaliana conferredan increased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 8073 in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “integral membraneprotein localized to late Golgi vesicles” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 8263 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “integral membrane protein localizedto late Golgi vesicles” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 8263 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “integral membrane protein localizedto late Golgi vesicles” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 8263 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “peptide transporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8287in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “peptide transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 8287 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “peptide transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 8287 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transcription factor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8468in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transcription factor” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 8468 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transcription factor” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 8468 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transmembrane proteinwith a role in cell wall polymer composition” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8484 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transmembrane protein with a rolein cell wall polymer composition” encoded by a gene comprising thenucleic acid sequence SEQ ID NO.: 8484 in Arabidopsis thaliana conferredan increased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transmembrane protein with a rolein cell wall polymer composition” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 8484 in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yll014w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8492in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll014w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8492 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll014w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8492 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “non-essential Rasguanine nucleotide exchange factor” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 8514 in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential Ras guaninenucleotide exchange factor” encoded by a gene comprising the nucleicacid sequence SEQ ID NO.: 8514 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential Ras guaninenucleotide exchange factor” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 8514 in Arabidopsis thaliana conferred anincreased NUE and an increased biomass production compared with the wildtype control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yll023c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8539in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll023c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8539 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll023c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8539 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yll037w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8571in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll037w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8571 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll037w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8571 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yll049w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8575in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll049w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8575 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yll049w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8575 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “cysteine transporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8579in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cysteine transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 8579 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cysteine transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 8579 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “metal iontransporter” encoded by a gene comprising the nucleic acid sequence SEQID NO. 8661 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “metal ion transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 8661 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “metal ion transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 8661 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ylr042c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8991in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr042c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8991 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr042c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8991 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YLR053c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 8995in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YLR053c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 8995 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YLR053c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 8995 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “cytosolic serinehydroxymethyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 8999 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cytosolic serinehydroxymethyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 8999 in Arabidopsis thaliana conferred an increasedbiomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cytosolic serinehydroxymethyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 8999 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “subunit ofcytoplasmic phenylalanyl-tRNA synthetase” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 9551 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “subunit of cytoplasmicphenylalanyl-tRNA synthetase” encoded by a gene comprising the nucleicacid sequence SEQ ID NO.: 9551 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “subunit of cytoplasmicphenylalanyl-tRNA synthetase” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 9551 in Arabidopsis thaliana conferred anincreased NUE and an increased biomass production compared with the wildtype control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ylr065c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 9637in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr065c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 9637 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr065c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 9637 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “xylitoldehydrogenase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 9672 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “xylitol dehydrogenase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 9672 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “xylitol dehydrogenase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 9672 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “3-keto sterolreductase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 10182 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “3-keto sterol reductase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO.: 10182 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “3-keto sterol reductase” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 10182 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “alkyl hydroperoxidereductase” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 10214 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alkyl hydroperoxide reductase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 10214in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alkyl hydroperoxide reductase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 10214in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ylr125w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 10447in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr125w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 10447 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr125w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 10447 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “anaphase promotingcomplex (APC) subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 10451 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “anaphase promoting complex (APC)subunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 10451 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “anaphase promoting complex (APC)subunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 10451 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein component ofthe large ribosomal subunit” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 10463 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein component of the largeribosomal subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO.: 10463 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein component of the largeribosomal subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 10463 in Arabidopsis thaliana conferred an increasedNUE and an increased biomass production compared with the wild typecontrol.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “mitochondrialprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 10533 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 10533 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “mitochondrial protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 10533 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ARV1 protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 10541 inArabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ARV1 protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 10541 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ARV1 protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 10541 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “GTP-binding protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 10562in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “GTP-binding protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 10562 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “GTP-binding protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 10562 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein involved inshmoo formation and bipolar bud site selection” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 10990 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein involved in shmoo formationand bipolar bud site selection” encoded by a gene comprising the nucleicacid sequence SEQ ID NO.: 10990 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein involved in shmoo formationand bipolar bud site selection” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 10990 in Arabidopsis thaliana conferred anincreased NUE and an increased biomass production compared with the wildtype control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “non-essentialkinetochore protein” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 10998 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential kinetochore protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 10998in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential kinetochore protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 10998in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Meiotic recombinationprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 11004 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Meiotic recombination protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 11004in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Meiotic recombination protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11004in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “signal transducingMEK kinase” encoded by a gene comprising the nucleic acid sequence SEQID NO. 11012 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “signal transducing MEK kinase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 11012in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “signal transducing MEK kinase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11012in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “cytochrome c oxidasesubunit VIII” encoded by a gene comprising the nucleic acid sequence SEQID NO. 11054 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cytochrome c oxidase subunit VIII”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 11054in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “cytochrome c oxidase subunit VIII”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11054in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ylr404w-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11066in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr404w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 11066 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr404w-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 11066 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ylr463c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11074in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr463c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 11074 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ylr463c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 11074 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “adeninephosphoribosyltransferase” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 11080 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “adenine phosphoribosyltransferase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 11080in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “adenine phosphoribosyltransferase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11080in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Mcm1p bindingtranscriptional repressor” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 11552 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Mcm1p binding transcriptionalrepressor” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 11552 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Mcm1p binding transcriptionalrepressor” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 11552 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “origin recognitioncomplex subunit” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 11569 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “origin recognition complex subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 11569in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “origin recognition complex subunit”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11569in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yml089c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11596in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yml089c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 11596 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yml089c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 11596 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “yml128c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11600in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yml128c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 11600 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “yml128c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 11600 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “hexose transporter”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 11612in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hexose transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 11612 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “hexose transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 11612 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Zinc finger protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12246in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Zinc finger protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 12246 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Zinc finger protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 12246 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein required formaturation of ribosomal RNAs” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 12263 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein required for maturation ofribosomal RNAs” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO.: 12263 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein required for maturation ofribosomal RNAs” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 12263 in Arabidopsis thaliana conferred an increased NUE andan increased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Factor arrestprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 12316 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Factor arrest protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 12316 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Factor arrest protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 12316 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR082C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12327in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR082C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 12327 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR082C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 12327 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Nuclear cap-bindingprotein complex subunit” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 12331 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Nuclear cap-binding protein complexsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 12331 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Nuclear cap-binding protein complexsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 12331 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR126c membraneprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 12378 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR126c membrane protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 12378 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR126c membrane protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 12378 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR144W-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12394in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR144W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 12394 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR144W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 12394 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR160W-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12406in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR160W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 12406 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR160W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 12406 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Stationary phaseprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 12414 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Stationary phase protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 12414 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Stationary phase protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 12414 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR209C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12420in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR209C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 12420 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR209C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 12420 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR233W-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12440in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR233W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 12440 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR233W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 12440 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a“phosphoglucomutase/phosphomannomutase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 12470 in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a“phosphoglucomutase/phosphomannomutase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO.: 12470 in Arabidopsis thalianaconferred an increased biomass production compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a“phosphoglucomutase/phosphomannomutase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 12470 in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Regulatory CAT8protein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 12749 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Regulatory CAT8 protein” encoded bya gene comprising the nucleic acid sequence SEQ ID NO.: 12749 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Regulatory CAT8 protein” encoded bya gene comprising the nucleic acid sequence SEQ ID NO. 12749 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “translationalelongation factor EF-3 (HEF3)” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 12773 in Arabidopsis thaliana conferred anincreased yield, especially an increased NUE compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “translational elongation factorEF-3 (HEF3)” encoded by a gene comprising the nucleic acid sequence SEQID NO.: 12773 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “translational elongation factorEF-3 (HEF3)” encoded by a gene comprising the nucleic acid sequence SEQID NO. 12773 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YNL320W-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12829in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YNL320W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 12829 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YNL320W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 12829 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Chitin synthase 3complex protein” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 12883 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Chitin synthase 3 complex protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 12883in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Chitin synthase 3 complex protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12883in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Alkyl/aryl-sulfatase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 12889in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Alkyl/aryl-sulfatase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 12889 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Alkyl/aryl-sulfatase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 12889 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “antiviral adaptorprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 13014 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “antiviral adaptor protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 13014 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “antiviral adaptor protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 13014 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “repressor of G1transcription” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 13018 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “repressor of G1 transcription”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 13018in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “repressor of G1 transcription”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 13018in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YOR097c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 13024in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YOR097c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 13024 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YOR097c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 13024 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a“Phosphoribosylaminoimidazole carboxylase” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 13030 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Phosphoribosylaminoimidazolecarboxylase” encoded by a gene comprising the nucleic acid sequence SEQID NO.: 13030 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Phosphoribosylaminoimidazolecarboxylase” encoded by a gene comprising the nucleic acid sequence SEQID NO. 13030 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “component of the RAMsignaling network” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 14085 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “component of the RAM signalingnetwork” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 14085 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “component of the RAM signalingnetwork” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 14085 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein kinase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14093in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein kinase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14093 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein kinase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14093 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “signal recognitionparticle subunit (SRP54)” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 14113 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “signal recognition particle subunit(SRP54)” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 14113 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “signal recognition particle subunit(SRP54)” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 14113 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “regulatory subunit ofthe 26S proteasome” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 14246 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “regulatory subunit of the 26Sproteasome” encoded by a gene comprising the nucleic acid sequence SEQID NO.: 14246 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “regulatory subunit of the 26Sproteasome” encoded by a gene comprising the nucleic acid sequence SEQID NO. 14246 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “RNA polymerase IIIsubunit” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 14311 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “RNA polymerase III subunit” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 14311 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “RNA polymerase III subunit” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 14311 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “lysophospholipase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14914in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysophospholipase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 14914 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “lysophospholipase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 14914 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “saccharopinedehydrogenase” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 15382 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “saccharopine dehydrogenase” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 15382 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “saccharopine dehydrogenase” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 15382 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “alpha-mannosidase”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15460in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alpha-mannosidase” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 15460 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “alpha-mannosidase” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 15460 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ykl100c-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15571in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykl100c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 15571 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ykl100c-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 15571 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “regulatory subunit ofGlc7p type 1 protein serine-threonine phosphatase” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 15593 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “regulatory subunit of Glc7p type 1protein serine-threonine phosphatase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO.: 15593 in Arabidopsis thalianaconferred an increased biomass production compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “regulatory subunit of Glc7p type 1protein serine-threonine phosphatase” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 15593 in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “non-essential Rasguanine nucleotide exchange factor” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 15646 in Arabidopsis thaliana conferredan increased yield, especially an increased NUE compared with the wildtype control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential Ras guaninenucleotide exchange factor” encoded by a gene comprising the nucleicacid sequence SEQ ID NO.: 15646 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “non-essential Ras guaninenucleotide exchange factor” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 15646 in Arabidopsis thaliana conferred anincreased NUE and an increased biomass production compared with the wildtype control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “metal iontransporter” encoded by a gene comprising the nucleic acid sequence SEQID NO. 15673 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “metal ion transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 15673 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “metal ion transporter” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 15673 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “subunit ofcytoplasmic phenylalanyl-tRNA synthetase” encoded by a gene comprisingthe nucleic acid sequence SEQ ID NO. 16005 in Arabidopsis thalianaconferred an increased yield, especially an increased NUE compared withthe wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “subunit of cytoplasmicphenylalanyl-tRNA synthetase” encoded by a gene comprising the nucleicacid sequence SEQ ID NO.: 16005 in Arabidopsis thaliana conferred anincreased biomass production compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “subunit of cytoplasmicphenylalanyl-tRNA synthetase” encoded by a gene comprising the nucleicacid sequence SEQ ID NO. 16005 in Arabidopsis thaliana conferred anincreased NUE and an increased biomass production compared with the wildtype control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YMR082C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16114in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR082C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 16114 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YMR082C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 16114 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “B1258-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14402in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B1258-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14402 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B1258-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14402 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YML101C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16093in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YML101C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 16093 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YML101C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 16093 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “nuclear fusionprotein precursor” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 16106 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “nuclear fusion protein precursor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 16106in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “nuclear fusion protein precursor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16106in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “inheritance ofperoxisomes protein” encoded by a gene comprising the nucleic acidsequence SEQ ID NO. 16120 in Arabidopsis thaliana conferred an increasedyield, especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “inheritance of peroxisomes protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 16120in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “inheritance of peroxisomes protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16120in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “exoribonuclease”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16275in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “exoribonuclease” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 16275 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “exoribonuclease” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 16275 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “iron sulfur clusterassembly protein” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 16305 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “iron sulfur cluster assemblyprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 16305 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “iron sulfur cluster assemblyprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 16305 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YPL068C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16573in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YPL068C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 16573 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YPL068C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 16573 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “B0165-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14396in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B0165-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14396 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B0165-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14396 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YOR203W-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16299in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YOR203W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 16299 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YOR203W-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 16299 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “ribonucleoprotein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 16133in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ribonucleoprotein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 16133 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “ribonucleoprotein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 16133 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transcription factor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15056in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transcription factor” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 15056 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transcription factor” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 15056 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YKL111C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15587in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YKL111C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 15587 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YKL111C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 15587 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “iron sulfur clusterassembly protein” encoded by a gene comprising the nucleic acid sequenceSEQ ID NO. 16582 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “iron sulfur cluster assemblyprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO.: 16582 in Arabidopsis thaliana conferred an increased biomassproduction compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “iron sulfur cluster assemblyprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 16582 in Arabidopsis thaliana conferred an increased NUE and anincreased biomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transport protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14839in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transport protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 14839 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transport protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 14839 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “protein translocaseprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 15014 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein translocase protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 15014in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “protein translocase protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15014in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YJL010C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15432in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YJL010C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 15432 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YJL010C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 15432 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “B1267-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14497in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B1267-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14497 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B1267-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14497 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “membrane protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14718in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “membrane protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14718 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “membrane protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14718 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “B1381-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14791in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B1381-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14791 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B1381-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14791 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “B2646-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 14879in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B2646-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 14879 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “B2646-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 14879 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “60S ribosomalprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 15064 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “60S ribosomal protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO.: 15064 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “60S ribosomal protein” encoded by agene comprising the nucleic acid sequence SEQ ID NO. 15064 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Rho GDP-dissociationinhibitor” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 15257 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Rho GDP-dissociation inhibitor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO.: 15257in Arabidopsis thaliana conferred an increased biomass productioncompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Rho GDP-dissociation inhibitor”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15257in Arabidopsis thaliana conferred an increased NUE and an increasedbiomass production compared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “YHL005C-protein”encoded by a gene comprising the nucleic acid sequence SEQ ID NO. 15378in Arabidopsis thaliana conferred an increased yield, especially anincreased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YHL005C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO.: 15378 in Arabidopsisthaliana conferred an increased biomass production compared with thewild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “YHL005C-protein” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 15378 in Arabidopsisthaliana conferred an increased NUE and an increased biomass productioncompared with the wild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “transmembrane proteinwith a role in cell wall polymer composition” encoded by a genecomprising the nucleic acid sequence SEQ ID NO. 16629 in Arabidopsisthaliana conferred an increased yield, especially an increased NUEcompared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “transmembrane protein with a rolein cell wall polymer composition” encoded by a gene comprising thenucleic acid sequence SEQ ID NO.: 16629 in Arabidopsis thalianaconferred an increased biomass production compared with the wild typecontrol.

It was further observed that increasing or generating the activity of agene product with the activity of a “transmembrane protein with a rolein cell wall polymer composition” encoded by a gene comprising thenucleic acid sequence SEQ ID NO. 16629 in Arabidopsis thaliana conferredan increased NUE and an increased biomass production compared with thewild type control.

In particular, it was observed that increasing or generating theactivity of a gene product with the activity of a “Stationary phaseprotein” encoded by a gene comprising the nucleic acid sequence SEQ IDNO. 16647 in Arabidopsis thaliana conferred an increased yield,especially an increased NUE compared with the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Stationary phase protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO.: 16647 inArabidopsis thaliana conferred an increased biomass production comparedwith the wild type control.

It was further observed that increasing or generating the activity of agene product with the activity of a “Stationary phase protein” encodedby a gene comprising the nucleic acid sequence SEQ ID NO. 16647 inArabidopsis thaliana conferred an increased NUE and an increased biomassproduction compared with the wild type control.

Thus, according to the method of the invention an enhanced NUE and/orincreased biomass production in a plant cell, plant or a part thereofcompared to a control or wild type can be achieved.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 39, or encoded by a nucleic acidmolecule comprising the nucleic acid SEQ ID NO. 38 or a nucleic acidwhich differs from the nucleic acid SEQ ID NO. 38 by exchanging the stopcodon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 38 or polypeptide SEQ ID NO. 39, respectivelyis increased or generated or if the activity “b0017-protein” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 43, or encoded by a nucleic acidmolecule comprising the nucleic acid SEQ ID NO. 42 or a homolog of saidnucleic acid molecule or polypeptide, e.g. if the activity of a nucleicacid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 42 orpolypeptide SEQ ID NO. 43, respectively is increased or generated or ifthe activity “transport protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 124, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 123 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 123 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 123 or polypeptide SEQ ID NO. 124, respectivelyis increased or generated or if the activity “hydroxymyristol acylcarrier protein dehydratase” is increased or generated in an organism,an increased yield, preferably an enhanced NUE and/or an increasedbiomass production compared with the wild type control is conferred insaid organism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 381, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 380 or a homolog ofsaid nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 380 orpolypeptide SEQ ID NO. 381, respectively is increased or generated or ifthe activity “gamma-glutamyl kinase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 680, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 679 or a homolog ofsaid nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 679 orpolypeptide SEQ ID NO. 680, respectively is increased or generated or ifthe activity “alpha-glucosidase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 813, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 812 or a homolog ofsaid nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 812 orpolypeptide SEQ ID NO. 813, respectively is increased or generated or ifthe activity “adenylate kinase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 1056, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 1055 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 1055 orpolypeptide SEQ ID NO. 1056, respectively is increased or generated orif the activity “2-dehydro-3-deoxy-phosphoheptonate aldolase” isincreased or generated in an organism, an increased yield, preferably anenhanced

NUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 1564, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 1563 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 1563 orpolypeptide SEQ ID NO. 1564, respectively is increased or generated orif the activity “molybdopterin biosynthesis protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 1706, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 1705 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 1705 orpolypeptide SEQ ID NO. 1706, respectively is increased or generated orif the activity “hydroxylamine reductase” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 1845, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 1844 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 1844 orpolypeptide SEQ ID NO. 1845, respectively is increased or generated orif the activity “proline dehydrogenase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 1951, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 1950 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 1950 orpolypeptide SEQ ID NO. 1951, respectively is increased or generated orif the activity “PhoH-like protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 1976, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 1975 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 1975 orpolypeptide SEQ ID NO. 1976, respectively is increased or generated orif the activity “isomerase” is increased or generated in an organism, anincreased yield, preferably an enhanced NUE and/or an increased biomassproduction compared with the wild type control is conferred in saidorganism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2128, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2127 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 2127 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2127 or polypeptide SEQ ID NO. 2128,respectively is increased or generated or if the activity“b1933-protein” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2136, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2135 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 2135 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2135 or polypeptide SEQ ID NO. 2136,respectively is increased or generated or if the activity“glycosyltransferase” is increased or generated in an organism, anincreased yield, preferably an enhanced NUE and/or an increased biomassproduction compared with the wild type control is conferred in saidorganism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2172, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2171 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 2171 orpolypeptide SEQ ID NO. 2172, respectively is increased or generated orif the activity “b2165-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2298, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2297 or a nucleicacid which differs from the nucleic acid SEQ

ID NO. 2297 by exchanging the stop codon taa by tga or a homolog of saidnucleic acid molecule or polypeptide, e.g. if the activity of a nucleicacid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 2297 orpolypeptide SEQ ID NO. 2298, respectively is increased or generated orif the activity “short chain fatty acid transporter” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2427, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2426 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 2426 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2426 or polypeptide SEQ ID NO. 2427,respectively is increased or generated or if the activity“b2238-protein” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2453, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2452 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 2452 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 2452 or polypeptide SEQ ID NO. 2453,respectively is increased or generated or if the activity“lysine/arginine/ornithine transporter subunit” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2552, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2551 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 2551 orpolypeptide SEQ ID NO. 2552, respectively is increased or generated orif the activity “b2431-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2601, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2600 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 2600 orpolypeptide SEQ ID NO. 2601, respectively is increased or generated orif the activity “chorismate mutase T/prephenate dehydrogenase(bifunctional)” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2669, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2668 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 2668 orpolypeptide SEQ ID NO. 2669, respectively is increased or generated orif the activity “b2766-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 2773, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 2772 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 2772 orpolypeptide SEQ ID NO. 2773, respectively is increased or generated orif the activity “glycine decarboxylase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3118, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3117 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3117 orpolypeptide SEQ ID NO. 3118, respectively is increased or generated orif the activity “threonine ammonia-lyase” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3391, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3390 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 3390 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3390 or polypeptide SEQ ID NO. 3391,respectively is increased or generated or if the activity“b3120-protein” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3397, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3396 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3396 orpolypeptide SEQ ID NO. 3397, respectively is increased or generated orif the activity “outer membrane usher protein” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3471, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3470 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3470 orpolypeptide SEQ ID NO. 3471, respectively is increased or generated orif the activity “glycerol-3-phosphate transporter subunit” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3564, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3563 or a nucleicacid which differs from the nucleic acid SEQ ID NO. 3563 by exchangingthe stop codon taa by tga or a homolog of said nucleic acid molecule orpolypeptide, e.g. if the activity of a nucleic acid molecule or apolypeptide comprising the nucleic acid or polypeptide or the consensussequence or the polypeptide motif, as depicted in Table I, II or IV,application no. 1, column 7 in the respective same line as the nucleicacid molecule SEQ ID NO. 3563 or polypeptide SEQ ID NO. 3564,respectively is increased or generated or if the activity “hydro-lyase”is increased or generated in an organism, an increased yield, preferablyan enhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3771, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3770 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3770 orpolypeptide SEQ ID NO. 3771, respectively is increased or generated orif the activity “lysophospholipase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3869, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3868 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3868 orpolypeptide SEQ ID NO. 3869, respectively is increased or generated orif the activity “yal019w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3896, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3895 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3895 orpolypeptide SEQ ID NO. 3896, respectively is increased or generated orif the activity “carnitine acetyltransferase” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 3954, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 3953 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 3953 orpolypeptide SEQ ID NO. 3954, respectively is increased or generated orif the activity “Transcriptional activator” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4112, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4111 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4111 orpolypeptide SEQ ID NO. 4112, respectively is increased or generated orif the activity “splicing factor” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4150, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4149 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4149 orpolypeptide SEQ ID NO. 4150, respectively is increased or generated orif the activity “autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit” is increased or generated in an organism, anincreased yield, preferably an enhanced NUE and/or an increased biomassproduction compared with the wild type control is conferred in saidorganism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4163, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4162 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4162 orpolypeptide SEQ ID NO. 4163, respectively is increased or generated orif the activity “microsomal beta-keto-reductase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4236, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4235 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4235 orpolypeptide SEQ ID NO. 4236, respectively is increased or generated orif the activity “UDP-N-acetyl-glucosamine-1-P transferase” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4281, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4280 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4280 orpolypeptide SEQ ID NO. 4281, respectively is increased or generated orif the activity “ybr262c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4289, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4288 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4288 orpolypeptide SEQ ID NO. 4289, respectively is increased or generated orif the activity “protein necessary for structural stability of L-Adouble-stranded RNA-containing particles” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4316, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4315 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4315 orpolypeptide SEQ ID NO. 4316, respectively is increased or generated orif the activity “YDR070C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4326, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4325 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4325 orpolypeptide SEQ ID NO. 4326, respectively is increased or generated orif the activity “chaperone” is increased or generated in an organism, anincreased yield, preferably an enhanced NUE and/or an increased biomassproduction compared with the wild type control is conferred in saidorganism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4336, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4335 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4335 orpolypeptide SEQ ID NO. 4336, respectively is increased or generated orif the activity “helix-loop-helix transcription activator that bindsinositol/choline-responsive elements” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4347, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4346 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4346 orpolypeptide SEQ ID NO. 4347, respectively is increased or generated orif the activity “golgi membrane exchange factor subunit” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4362, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4361 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4361 orpolypeptide SEQ ID NO. 4362, respectively is increased or generated orif the activity “dihydrosphingosine phosphate lyase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4403, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4402 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4402 orpolypeptide SEQ ID NO. 4403, respectively is increased or generated orif the activity “ubiquitin regulatory protein” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4432, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4431 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4431 orpolypeptide SEQ ID NO. 4432, respectively is increased or generated orif the activity “ydr355c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4436, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4435 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4435 orpolypeptide SEQ ID NO. 4436, respectively is increased or generated orif the activity “lysine-specific metalloprotease” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4486, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4485 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4485 orpolypeptide SEQ ID NO. 4486, respectively is increased or generated orif the activity “subunit of the transport protein particle (TRAPP)complex of the cis-Golgi” is increased or generated in an organism, anincreased yield, preferably an enhanced NUE and/or an increased biomassproduction compared with the wild type control is conferred in saidorganism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4507, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4506 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4506 orpolypeptide SEQ ID NO. 4507, respectively is increased or generated orif the activity “myo-inositol transporter” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4791, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4790 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4790 orpolypeptide SEQ ID NO. 4791, respectively is increased or generated orif the activity “SM complex B protein for mRNA splicing” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4807, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4806 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4806 orpolypeptide SEQ ID NO. 4807, respectively is increased or generated orif the activity “YFR007W-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 4837, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 4836 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 4836 orpolypeptide SEQ ID NO. 4837, respectively is increased or generated orif the activity “oxidoreductase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5312, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5311 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5311 orpolypeptide SEQ ID NO. 5312, respectively is increased or generated orif the activity “transcription elongation factor” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5347, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5346 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5346 orpolypeptide SEQ ID NO. 5347, respectively is increased or generated orif the activity “cytosolic catalase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5534, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5533 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5533 orpolypeptide SEQ ID NO. 5534, respectively is increased or generated orif the activity “ygr122c-a-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5552, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5551 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5551 orpolypeptide SEQ ID NO. 5552, respectively is increased or generated orif the activity “v-SNARE binding protein” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5560, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5559 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5559 orpolypeptide SEQ ID NO. 5560, respectively is increased or generated orif the activity “protein involved in sphingolipid biosynthesis” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5603, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5602 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5602 orpolypeptide SEQ ID NO. 5603, respectively is increased or generated orif the activity “mitochondrial ribosomal protein of the small subunit”is increased or generated in an organism, an increased yield, preferablyan enhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5609, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5608 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5608 orpolypeptide SEQ ID NO. 5609, respectively is increased or generated orif the activity “phosphatidylserine decarboxylase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5615, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5614 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5614 orpolypeptide SEQ ID NO. 5615, respectively is increased or generated orif the activity “cholinephosphate cytidylyltransferase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5667, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5666 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5666 orpolypeptide SEQ ID NO. 5667, respectively is increased or generated orif the activity “ygr266w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5702, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5701 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5701 orpolypeptide SEQ ID NO. 5702, respectively is increased or generated orif the activity “cell wall endo-beta-1,3-glucanase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5751, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5750 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5750 orpolypeptide SEQ ID NO. 5751, respectively is increased or generated orif the activity “ygr290w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5755, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5754 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5754 orpolypeptide SEQ ID NO. 5755, respectively is increased or generated orif the activity “yhl021c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5779, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5778 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5778 orpolypeptide SEQ ID NO. 5779, respectively is increased or generated orif the activity “v-SNARE protein involved in Golgi transport” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5813, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5812 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5812 orpolypeptide SEQ ID NO. 5813, respectively is increased or generated orif the activity “mitochondrial seryl-tRNA synthetase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5968, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5967 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5967 orpolypeptide SEQ ID NO. 5968, respectively is increased or generated orif the activity “yhr127w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 5974, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 5973 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 5973 orpolypeptide SEQ ID NO. 5974, respectively is increased or generated orif the activity “aromatic amino acid aminotransferase II” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6028, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6027 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6027 orpolypeptide SEQ ID NO. 6028, respectively is increased or generated orif the activity “glucoamylase” is increased or generated in an organism,an increased yield, preferably an enhanced NUE and/or an increasedbiomass production compared with the wild type control is conferred insaid organism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6108, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6107 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6107 orpolypeptide SEQ ID NO. 6108, respectively is increased or generated orif the activity “histidine kinase osmosensor that regulates anosmosensing MAP kinase cascade” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6151, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6150 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6150 orpolypeptide SEQ ID NO. 6151, respectively is increased or generated orif the activity “saccharopine dehydrogenase” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6199, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6198 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6198 orpolypeptide SEQ ID NO. 6199, respectively is increased or generated orif the activity “spindle checkpoint complex subunit” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6209, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6208 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6208 orpolypeptide SEQ ID NO. 6209, respectively is increased or generated orif the activity “nuclear pore complex subunit” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6243, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6242 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6242 orpolypeptide SEQ ID NO. 6243, respectively is increased or generated orif the activity “yjl064w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6247, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6246 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6246 orpolypeptide SEQ ID NO. 6247, respectively is increased or generated orif the activity “yjl067w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6251, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6250 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6250 orpolypeptide SEQ ID NO. 6251, respectively is increased or generated orif the activity “potassium:hydrogen antiporter” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6298, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6297 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6297 orpolypeptide SEQ ID NO. 6298, respectively is increased or generated orif the activity “GPI-anchored cell wall protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6327, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6326 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6326 orpolypeptide SEQ ID NO. 6327, respectively is increased or generated orif the activity “yjl213w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6489, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6488 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6488 orpolypeptide SEQ ID NO. 6489, respectively is increased or generated orif the activity “peptidyl-prolyl cis-trans isomerase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6551, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6550 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6550 orpolypeptide SEQ ID NO. 6551, respectively is increased or generated orif the activity “clathrin associated protein complex small subunit” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6701, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6700 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6700 orpolypeptide SEQ ID NO. 6701, respectively is increased or generated orif the activity “zinc metalloprotease” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 6817, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 6816 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 6816 orpolypeptide SEQ ID NO. 6817, respectively is increased or generated orif the activity “F1F0 ATP synthase beta subunit” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7367, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7366 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7366 orpolypeptide SEQ ID NO. 7367, respectively is increased or generated orif the activity “alpha-mannosidase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7476, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7475 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7475 orpolypeptide SEQ ID NO. 7476, respectively is increased or generated orif the activity “ribosomal protein of the small subunit” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7603, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7602 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7602 orpolypeptide SEQ ID NO. 7603, respectively is increased or generated orif the activity “mitochondrial intermembrane space protein” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7652, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7651 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7651 orpolypeptide SEQ ID NO. 7652, respectively is increased or generated orif the activity “phosphopantothenoylcysteine decarboxylase” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7662, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7661 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7661 orpolypeptide SEQ ID NO. 7662, respectively is increased or generated orif the activity “ykl100c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7676, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7675 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7675 orpolypeptide SEQ ID NO. 7676, respectively is increased or generated orif the activity “ykl131w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7680, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7679 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7679 orpolypeptide SEQ ID NO. 7680, respectively is increased or generated orif the activity “mitochondrial ribosomal protein of the large subunit”is increased or generated in an organism, an increased yield, preferablyan enhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7711, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7710 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7710 orpolypeptide SEQ ID NO. 7711, respectively is increased or generated orif the activity “G protein coupled pheromone receptor receptor” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7736, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7735 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7735 orpolypeptide SEQ ID NO. 7736, respectively is increased or generated orif the activity “golgi membrane protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7779, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7778 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7778 orpolypeptide SEQ ID NO. 7779, respectively is increased or generated orif the activity “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase” is increased or generated in an organism,an increased yield, preferably an enhanced NUE and/or an increasedbiomass production compared with the wild type control is conferred insaid organism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 7830, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 7829 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 7829 orpolypeptide SEQ ID NO. 7830, respectively is increased or generated orif the activity “dihydroorotate dehydrogenase” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8018, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8017 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8017 orpolypeptide SEQ ID NO. 8018, respectively is increased or generated orif the activity “ykr016w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8046, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8045 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8045 orpolypeptide SEQ ID NO. 8046, respectively is increased or generated orif the activity “ykr021w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8074, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8073 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8073 orpolypeptide SEQ ID NO. 8074, respectively is increased or generated orif the activity “non-essential small GTPase of the Rho/Rac subfamily ofRas-like proteins” is increased or generated in an organism, anincreased yield, preferably an enhanced NUE and/or an increased biomassproduction compared with the wild type control is conferred in saidorganism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8264, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8263 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8263 orpolypeptide SEQ ID NO. 8264, respectively is increased or generated orif the activity “integral membrane protein localized to late Golgivesicles” is increased or generated in an organism, an increased yield,preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8288, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8287 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8287 orpolypeptide SEQ ID NO. 8288, respectively is increased or generated orif the activity “peptide transporter” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8469, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8468 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8468 orpolypeptide SEQ ID NO. 8469, respectively is increased or generated orif the activity “transcription factor” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8485, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8484 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8484 orpolypeptide SEQ ID NO. 8485, respectively is increased or generated orif the activity “transmembrane protein with a role in cell wall polymercomposition” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8493, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8492 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8492 orpolypeptide SEQ ID NO. 8493, respectively is increased or generated orif the activity “yll014w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8515, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8514 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8514 orpolypeptide SEQ ID NO. 8515, respectively is increased or generated orif the activity “non-essential Ras guanine nucleotide exchange factor”is increased or generated in an organism, an increased yield, preferablyan enhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8540, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8539 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8539 orpolypeptide SEQ ID NO. 8540, respectively is increased or generated orif the activity “yll023c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8572, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8571 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8571 orpolypeptide SEQ ID NO. 8572, respectively is increased or generated orif the activity “yll037w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8576, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8575 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8575 orpolypeptide SEQ ID NO. 8576, respectively is increased or generated orif the activity “yll049w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8580, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8579 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8579 orpolypeptide SEQ ID NO. 8580, respectively is increased or generated orif the activity “cysteine transporter” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8662, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8661 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8661 orpolypeptide SEQ ID NO. 8662, respectively is increased or generated orif the activity “metal ion transporter” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8992, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8991 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8991 orpolypeptide SEQ ID NO. 8992, respectively is increased or generated orif the activity “ylr042c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 8996, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8995 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8995 orpolypeptide SEQ ID NO. 8996, respectively is increased or generated orif the activity “YLR053c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 9000, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 8999 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 8999 orpolypeptide SEQ ID NO. 9000, respectively is increased or generated orif the activity “cytosolic serine hydroxymethyltransferase” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 9552, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 9551 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 9551 orpolypeptide SEQ ID NO. 9552, respectively is increased or generated orif the activity “subunit of cytoplasmic phenylalanyl-tRNA synthetase” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 9638, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 9637 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 9637 orpolypeptide SEQ ID NO. 9638, respectively is increased or generated orif the activity “ylr065c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 9673, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 9672 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 9672 orpolypeptide SEQ ID NO. 9673, respectively is increased or generated orif the activity “xylitol dehydrogenase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10183, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10182 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10182 orpolypeptide SEQ ID NO. 10183, respectively is increased or generated orif the activity “3-keto sterol reductase” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10215, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10214 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10214 orpolypeptide SEQ ID NO. 10215, respectively is increased or generated orif the activity “alkyl hydroperoxide reductase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10448, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10447 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10447 orpolypeptide SEQ ID NO. 10448, respectively is increased or generated orif the activity “ylr125w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10452, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10451 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10451 orpolypeptide SEQ ID NO. 10452, respectively is increased or generated orif the activity “anaphase promoting complex (APC) subunit” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10464, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10463 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10463 orpolypeptide SEQ ID NO. 10464, respectively is increased or generated orif the activity “protein component of the large ribosomal subunit”isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10534, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10533 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10533 orpolypeptide SEQ ID NO. 10534, respectively is increased or generated orif the activity “mitochondrial protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10542, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10541 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10541 orpolypeptide SEQ ID NO. 10542, respectively is increased or generated orif the activity “ARV1 protein” is increased or generated in an organism,an increased yield, preferably an enhanced NUE and/or an increasedbiomass production compared with the wild type control is conferred insaid organism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10563, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10562 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10562 orpolypeptide SEQ ID NO. 10563, respectively is increased or generated orif the activity “GTP-binding protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10991, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10990 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10990 orpolypeptide SEQ ID NO. 10991, respectively is increased or generated orif the activity “protein involved in shmoo formation and bipolar budsite selection” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 10999, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 10998 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 10998 orpolypeptide SEQ ID NO. 10999, respectively is increased or generated orif the activity “non-essential kinetochore protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11005, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11004 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11004 orpolypeptide SEQ ID NO. 11005, respectively is increased or generated orif the activity “Meiotic recombination protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11013, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11012 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11012 orpolypeptide SEQ ID NO. 11013, respectively is increased or generated orif the activity “signal transducing MEK kinase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11055, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11054 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11054 orpolypeptide SEQ ID NO. 11055, respectively is increased or generated orif the activity “cytochrome c oxidase subunit VIII” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11067, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11066 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11066 orpolypeptide SEQ ID NO. 11067, respectively is increased or generated orif the activity “ylr404w-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11075, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11074 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11074 orpolypeptide SEQ ID NO. 11075, respectively is increased or generated orif the activity “ylr463c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11081, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11080 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11080 orpolypeptide SEQ ID NO. 11081, respectively is increased or generated orif the activity “adenine phosphoribosyltransferase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11553, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11552 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11552 orpolypeptide SEQ ID NO. 11553, respectively is increased or generated orif the activity “Mcm1p binding transcriptional repressor” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11570, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11569 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11569 orpolypeptide SEQ ID NO. 11570, respectively is increased or generated orif the activity “origin recognition complex subunit” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11597, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11596 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11596 orpolypeptide SEQ ID NO. 11597, respectively is increased or generated orif the activity “yml089c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11601, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11600 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11600 orpolypeptide SEQ ID NO. 11601, respectively is increased or generated orif the activity “yml128c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 11613, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 11612 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 11612 orpolypeptide SEQ ID NO. 11613, respectively is increased or generated orif the activity “hexose transporter” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12247, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12246 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12246 orpolypeptide SEQ ID NO. 12247, respectively is increased or generated orif the activity “Zinc finger protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12264, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12263 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12263 orpolypeptide SEQ ID NO. 12264, respectively is increased or generated orif the activity “protein required for maturation of ribosomal RNAs” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12317, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12316 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12316 orpolypeptide SEQ ID NO. 12317, respectively is increased or generated orif the activity “Factor arrest protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12328, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12327 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12327 orpolypeptide SEQ ID NO. 12328, respectively is increased or generated orif the activity “YMR082C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12332, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12331 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12331 orpolypeptide SEQ ID NO. 12332, respectively is increased or generated orif the activity “Nuclear cap-binding protein complex subunit” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12379, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12378 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12378 orpolypeptide SEQ ID NO. 12379, respectively is increased or generated orif the activity “YMR126c membrane protein” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12395, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12394 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12394 orpolypeptide SEQ ID NO. 12395, respectively is increased or generated orif the activity “YMR144W-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12407, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12406 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12406 orpolypeptide SEQ ID NO. 12407, respectively is increased or generated orif the activity “YMR160W-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12415, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12414 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12414 orpolypeptide SEQ ID NO. 12415, respectively is increased or generated orif the activity “Stationary phase protein” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12421, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12420 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12420 orpolypeptide SEQ ID NO. 12421, respectively is increased or generated orif the activity “YMR209C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12441, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12440 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12440 orpolypeptide SEQ ID NO. 12441, respectively is increased or generated orif the activity “YMR233W-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12471, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12470 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12470 orpolypeptide SEQ ID NO. 12471, respectively is increased or generated orif the activity “phosphoglucomutase/phosphomannomutase” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12750, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12749 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12749 orpolypeptide SEQ ID NO. 12750, respectively is increased or generated orif the activity “Regulatory CAT8 protein” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12774, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12773 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12773 orpolypeptide SEQ ID NO. 12774, respectively is increased or generated orif the activity “translational elongation factor EF-3 (HEF3)” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12830, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12829 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12829 orpolypeptide SEQ ID NO. 12830, respectively is increased or generated orif the activity “YNL320W-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12884, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12883 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12883 orpolypeptide SEQ ID NO. 12884, respectively is increased or generated orif the activity “Chitin synthase 3 complex protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 12890, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 12889 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 12889 orpolypeptide SEQ ID NO. 12890, respectively is increased or generated orif the activity “Alkyl/aryl-sulfatase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 13015, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 13014 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 13014 orpolypeptide SEQ ID NO. 13015, respectively is increased or generated orif the activity “antiviral adaptor protein” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 13019, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 13018 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 13018 orpolypeptide SEQ ID NO. 13019, respectively is increased or generated orif the activity “repressor of G1 transcription” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 13025, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 13024 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 13024 orpolypeptide SEQ ID NO. 13025, respectively is increased or generated orif the activity “YOR097c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 13031, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 13030 or a homologof said nucleic acid molecule of an eukaryote or polypeptide, e.g. ifthe activity of a nucleic acid molecule or a polypeptide comprising thenucleic acid or polypeptide or the consensus sequence or the polypeptidemotif, as depicted in Table I, II or IV, application no. 1, column 7 inthe respective same line as the nucleic acid molecule SEQ ID NO. 13030or polypeptide SEQ ID NO. 13031, respectively is increased or generatedor if the activity “Phosphoribosylaminoimidazole carboxylase” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

In eukaryote the polypeptide is bifunctional and encoded by one nucleicacid molecule. Usually in prokaryote these two functions are encoded bytwo distinct nucleic acid molecules. The homologs of the respectivenucleic acid molecules are listed in tables IA NHOM, IA CHOM, IIA NHOMand IIA CHOM (NHOM for the nucleic acid molecule encoding for thepolypeptide covering the N-terminus and the polypeptide covering theN-terminus, respectively; CHOM for the nucleic acid molecule encodingfor the polypeptide covering the C-terminus and the polypeptide coveringthe C-terminus, respectively). The co-expression and/or expression of agene fusion of these homologs, which may be performed by methods knownto a skilled person, give the same results as the expression of theeukaryotic homologs.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14086, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14085 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14085 orpolypeptide SEQ ID NO. 14086, respectively is increased or generated orif the activity “component of the RAM signaling network” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14094, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14093 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14093 orpolypeptide SEQ ID NO. 14094, respectively is increased or generated orif the activity “protein kinase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14114, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14113 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14113 orpolypeptide SEQ ID NO. 14114, respectively is increased or generated orif the activity “signal recognition particle subunit (SRP54)” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14247, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14246 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14246 orpolypeptide SEQ ID NO. 14247, respectively is increased or generated orif the activity “regulatory subunit of the 26S proteasome” is increasedor generated in an organism, an increased yield, preferably an enhancedNUE and/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14312, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14311 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14311 orpolypeptide SEQ ID NO. 14312, respectively is increased or generated orif the activity “RNA polymerase III subunit” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14915, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14914 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14914 orpolypeptide SEQ ID NO. 14915, respectively is increased or generated orif the activity “lysophospholipase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15383, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15382 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15382 orpolypeptide SEQ ID NO. 15383, respectively is increased or generated orif the activity “saccharopine dehydrogenase” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15461, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15460 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15460 orpolypeptide SEQ ID NO. 15461, respectively is increased or generated orif the activity “alpha-mannosidase” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15572, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15571 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15571 orpolypeptide SEQ ID NO. 15572, respectively is increased or generated orif the activity “ykl100c-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15594, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15593 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15593 orpolypeptide SEQ ID NO. 15594, respectively is increased or generated orif the activity “regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase” is increased or generated in an organism,an increased yield, preferably an enhanced NUE and/or an increasedbiomass production compared with the wild type control is conferred insaid organism, especially an enhanced NUE, or an increased biomassproduction, or an enhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15647, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15646 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15646 orpolypeptide SEQ ID NO. 15647, respectively is increased or generated orif the activity “non-essential Ras guanine nucleotide exchange factor”is increased or generated in an organism, an increased yield, preferablyan enhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15674, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15673 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15673 orpolypeptide SEQ ID NO. 15674, respectively is increased or generated orif the activity “metal ion transporter” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16006, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16005 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16005 orpolypeptide SEQ ID NO. 16006, respectively is increased or generated orif the activity “subunit of cytoplasmic phenylalanyl-tRNA synthetase” isincreased or generated in an organism, an increased yield, preferably anenhanced NUE and/or an increased biomass production compared with thewild type control is conferred in said organism, especially an enhancedNUE, or an increased biomass production, or an enhanced NUE and anincreased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16115, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16114 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16114 orpolypeptide SEQ ID NO. 16115, respectively is increased or generated orif the activity “YMR082C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14403, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14402 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14402 orpolypeptide SEQ ID NO. 14403, respectively is increased or generated orif the activity “B1258-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16094, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16093 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16093 orpolypeptide SEQ ID NO. 16094, respectively is increased or generated orif the activity “YML101C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16107, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16106 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16106 orpolypeptide SEQ ID NO. 16107, respectively is increased or generated orif the activity “nuclear fusion protein precursor” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16121, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16120 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16120 orpolypeptide SEQ ID NO. 16121, respectively is increased or generated orif the activity “inheritance of peroxisomes protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16276, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16275 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16275 orpolypeptide SEQ ID NO. 16276, respectively is increased or generated orif the activity “exoribonuclease” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16306, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16305 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16305 orpolypeptide SEQ ID NO. 16306, respectively is increased or generated orif the activity “iron sulfur cluster assembly protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16574, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16573 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16573 orpolypeptide SEQ ID NO. 16574, respectively is increased or generated orif the activity “YPL068C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14397, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14396 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14396 orpolypeptide SEQ ID NO. 14397, respectively is increased or generated orif the activity “B0165-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16300, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16299 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16299 orpolypeptide SEQ ID NO. 16300, respectively is increased or generated orif the activity “YOR203W-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16134, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16133 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16133 orpolypeptide SEQ ID NO. 16134, respectively is increased or generated orif the activity “ribonucleoprotein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15057, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15056 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15056 orpolypeptide SEQ ID NO. 15057, respectively is increased or generated orif the activity “transcription factor” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15588, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15587 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15587 orpolypeptide SEQ ID NO. 15588, respectively is increased or generated orif the activity “YKL111C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16583, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16582 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16582 orpolypeptide SEQ ID NO. 16583, respectively is increased or generated orif the activity “iron sulfur cluster assembly protein” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14840, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14839 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14839 orpolypeptide SEQ ID NO. 14840, respectively is increased or generated orif the activity “transport protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15015, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15014 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15014 orpolypeptide SEQ ID NO. 15015, respectively is increased or generated orif the activity “protein translocase protein” is increased or generatedin an organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15433, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15432 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15432 orpolypeptide SEQ ID NO. 15433, respectively is increased or generated orif the activity “YJL010C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14498, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14497 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14497 orpolypeptide SEQ ID NO. 14498, respectively is increased or generated orif the activity “B1267-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14719, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14718 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14718 orpolypeptide SEQ ID NO. 14719, respectively is increased or generated orif the activity “membrane protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14792, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14791 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14791 orpolypeptide SEQ ID NO. 14792, respectively is increased or generated orif the activity “B1381-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 14880, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 14879 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 14879 orpolypeptide SEQ ID NO. 14880, respectively is increased or generated orif the activity “B2646-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15065, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15064 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15064 orpolypeptide SEQ ID NO. 15065, respectively is increased or generated orif the activity “60S ribosomal protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15258, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15257 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15257 orpolypeptide SEQ ID NO. 15258, respectively is increased or generated orif the activity “Rho GDP-dissociation inhibitor” is increased orgenerated in an organism, an increased yield, preferably an enhanced NUEand/or an increased biomass production compared with the wild typecontrol is conferred in said organism, especially an enhanced NUE, or anincreased biomass production, or an enhanced NUE and an increasedbiomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 15379, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 15378 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 15378 orpolypeptide SEQ ID NO. 15379, respectively is increased or generated orif the activity “YHL005C-protein” is increased or generated in anorganism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16630, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16629 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16629 orpolypeptide SEQ ID NO. 16630, respectively is increased or generated orif the activity “transmembrane protein with a role in cell wall polymercomposition” is increased or generated in an organism, an increasedyield, preferably an enhanced NUE and/or an increased biomass productioncompared with the wild type control is conferred in said organism,especially an enhanced NUE, or an increased biomass production, or anenhanced NUE and an increased biomass production.

Accordingly, in one embodiment, in case the activity of a polypeptideaccording to the polypeptide SEQ ID NO. 16648, or encoded by a nucleicacid molecule comprising the nucleic acid SEQ ID NO. 16647 or a homologof said nucleic acid molecule or polypeptide, e.g. if the activity of anucleic acid molecule or a polypeptide comprising the nucleic acid orpolypeptide or the consensus sequence or the polypeptide motif, asdepicted in Table I, II or IV, application no. 1, column 7 in therespective same line as the nucleic acid molecule SEQ ID NO. 16647 orpolypeptide SEQ ID NO. 16648, respectively is increased or generated orif the activity “Stationary phase protein” is increased or generated inan organism, an increased yield, preferably an enhanced NUE and/or anincreased biomass production compared with the wild type control isconferred in said organism, especially an enhanced NUE, or an increasedbiomass production, or an enhanced NUE and an increased biomassproduction.

It was further observed that increasing or generating the activity of anucleic acid molecule derived from the nucleic acid molecule shown intable VII-A in a plant, for example A. thaliana, conferred increasednutrient use efficiency, e.g. an increased the nitrogen use efficiency,compared with the wild type control. Thus, in one embodiment, a nucleicacid molecule indicated in table VII-A or its homolog as indicated intable I or the expression product is used in the method of the presentinvention to increase nutrient use efficiency, e.g. to increase thenitrogen use efficiency, of a plant compared with the wild type control.

It was further observed that increasing or generating the activity of anucleic acid molecule derived from the nucleic acid molecule shown intable VII-B in a plant, for example A. thaliana, conferred increasedstress tolerance, e.g. increased low temperature tolerance, comparedwith the wild type control. Thus, in one embodiment, a nucleic acidmolecule indicated in table VII-B or its homolog as indicated in table Ior the expression product is used in the method of the present inventionto increase stress tolerance, e.g. increase low temperature tolerance,of a plant compared with the wild type control.

It was further observed that increasing or generating the activity of anucleic acid molecule derived from the nucleic acid molecule shown intable VII-C in a plant, for example A. thaliana, conferred increasedstress tolerance, e.g. increased cycling drought tolerance, comparedwith the wild type control. Thus, in one embodiment, a nucleic acidmolecule indicated in table VII-C or its homolog as indicated in table Ior the expression product is used in the method of the present inventionto increase stress tolerance, e.g. increase cycling drought tolerance,of a plant compared with the wild type control.

It was further observed that increasing or generating the activity of anucleic acid molecule derived from the nucleic acid molecule shown inTable VII-D in a plant, for example A. thaliana, conferred increase inintrinsic yield, e.g. increased biomass under standard conditions, e.g.increased biomass in the absence of stress conditions as well as in theabsence of nutrient deficiency, compared with the wild type control.Thus, in one embodiment, a nucleic acid molecule indicated in tableVII-D or its homolog as indicated in table I or the expression productis used in the method of the present invention to increase intrinsicyield, e.g. to increase yield, in the absence of stress conditions aswell as in the absence of nutrient deficiency, of a plant compared withthe wild type control.

The term “expression” refers to the transcription and/or translation ofa codogenic gene segment or gene. As a rule, the resulting product is anmRNA or a protein. However, expression products can also includefunctional RNAs such as, for example, antisense, nucleic acids, tRNAs,snRNAs, rRNAs, RNAi, siRNA, ribozymes etc. Expression may be systemic,local or temporal, for example limited to certain cell types, tissuesorgans or organelles or time periods.

In one embodiment, the process of the present invention comprises one ormore of the following steps

-   (a) stabilizing a protein conferring the increased expression of a    protein encoded by the nucleic acid molecule of the invention or of    the polypeptide of the invention having the herein-mentioned    activity selected from the group consisting of    2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol    reductase, 60S ribosomal protein, adenine phosphoribosyltransferase,    adenylate kinase, alkyl hydroperoxide reductase,    Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase, anaphase    promoting complex (APC) subunit, antiviral adaptor protein, aromatic    amino acid aminotransferase II, ARV1 protein, autophagy-specific    phosphatidylinositol 3-kinase complex protein subunit,    b0017-protein, B0165-protein, B1258-protein, B1267-protein,    B1381-protein, b1933-protein, b2165-protein, b2238-protein,    b2431-protein, B2646-protein, b2766-protein, b3120-protein,    carnitine acetyltransferase, cell wall endo-beta-1,3-glucanase,    chaperone, Chitin synthase 3 complex protein, cholinephosphate    cytidylyltransferase, chorismate mutase T/prephenate dehydrogenase    (bifunctional), clathrin associated protein complex small subunit,    component of the RAM signaling network, cysteine transporter,    cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic    serine hydroxymethyltransferase, dihydroorotate dehydrogenase,    dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP    synthase beta subunit, Factor arrest protein, G protein coupled    pheromone receptor receptor, gamma-glutamyl kinase, glucoamylase,    glycerol-3-phosphate transporter subunit, glycine decarboxylase,    glycosyltransferase, golgi membrane exchange factor subunit, golgi    membrane protein, GPI-anchored cell wall protein, GTP-binding    protein, helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein,

YMR126c membrane protein, YMR144W-protein, YMR160W-protein,YMR209C-protein, YMR233W-protein, YNL320W-protein, YOR097c-protein,YOR203W-protein, YPL068C-protein, Zinc finger protein, and zincmetalloprotease and conferring an increased yield, especially anenhanced NUE and/or increased biomass production, as compared to acorresponding non-transformed wild type plant cell, plant or partthereof;

-   (b) stabilizing a mRNA conferring the increased expression of a    protein encoded by the nucleic acid molecule of the invention or its    homologs or of a mRNA encoding the polypeptide of the present    invention having the herein-mentioned activity selected from the    group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease and conferring an    increased yield, especially an enhanced NUE and/or increased biomass    production, as compared to a corresponding non-transformed wild type    plant cell, plant or part thereof;-   (c) increasing the specific activity of a protein conferring the    increased expression of a protein encoded by the nucleic acid    molecule of the invention or of the polypeptide of the present    invention or decreasing the inhibitory regulation of the polypeptide    of the invention;-   (d) generating or increasing the expression of an endogenous or    artificial transcription factor mediating the expression of a    protein conferring the increased expression of a protein encoded by    the nucleic acid molecule of the invention or of the polypeptide of    the invention having the herein-mentioned activity selected from the    group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease and conferring an    increased yield, especially an enhanced NUE and/or increased biomass    production, as compared to a corresponding non-transformed wild type    plant cell, plant or part thereof;-   (e) stimulating activity of a protein conferring the increased    expression of a protein encoded by the nucleic acid molecule of the    present invention or a polypeptide of the present invention having    the herein-mentioned activity selected from the group consisting of    2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-keto sterol    reductase, 60S ribosomal protein, adenine phosphoribosyltransferase,    adenylate kinase, alkyl hydroperoxide reductase,    Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase, anaphase    promoting complex (APC) subunit, antiviral adaptor protein, aromatic    amino acid aminotransferase II, ARV1 protein, autophagy-specific    phosphatidylinositol 3-kinase complex protein subunit,    b0017-protein, B0165-protein, B1258-protein, B1267-protein,    B1381-protein, b1933-protein, b2165-protein, b2238-protein,    b2431-protein, B2646-protein, b2766-protein, b3120-protein,    carnitine acetyltransferase, cell wall endo-beta-1,3-glucanase,    chaperone, Chitin synthase 3 complex protein, cholinephosphate    cytidylyltransferase, chorismate mutase T/prephenate dehydrogenase    (bifunctional), clathrin associated protein complex small subunit,    component of the RAM signaling network, cysteine transporter,    cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic    serine hydroxymethyltransferase, dihydroorotate dehydrogenase,    dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP    synthase beta subunit, Factor arrest protein, G protein coupled    pheromone receptor receptor, gamma-glutamyl kinase, glucoamylase,    glycerol-3-phosphate transporter subunit, glycine decarboxylase,    glycosyltransferase, golgi membrane exchange factor subunit, golgi    membrane protein, GPI-anchored cell wall protein, GTP-binding    protein, helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease and conferring an    increased yield, especially an enhanced NUE and/or increased biomass    production, as compared to a corresponding non-transformed wild type    plant cell, plant or part thereof by adding one or more exogenous    inducing factors to the organisms or parts thereof;-   (f) expressing a transgenic gene encoding a protein conferring the    increased expression of a polypeptide encoded by the nucleic acid    molecule of the present invention or a polypeptide of the present    invention, having the herein-mentioned activity selected from the    group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase,

Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase, anaphasepromoting complex (APC) subunit, antiviral adaptor protein, aromaticamino acid aminotransferase II, ARV1 protein, autophagy-specificphosphatidylinositol 3-kinase complex protein subunit, b0017-protein,B0165-protein, B1258-protein, 61267-protein, B1381-protein,b1933-protein, b2165-protein, b2238-protein, b2431-protein,B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease and conferring an increasedyield, especially an enhanced NUE and/or increased biomass production,as compared to a corresponding non-transformed wild type plant cell,plant or part thereof; and/or

-   (g) increasing the copy number of a gene conferring the increased    expression of a nucleic acid molecule encoding a polypeptide encoded    by the nucleic acid molecule of the invention or the polypeptide of    the invention having the herein-mentioned activity selected from the    group consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase,    3-keto sterol reductase, 60S ribosomal protein, adenine    phosphoribosyltransferase, adenylate kinase, alkyl hydroperoxide    reductase, Alkyl/aryl-sulfatase, alpha-glucosidase,    alpha-mannosidase, anaphase promoting complex (APC) subunit,    antiviral adaptor protein, aromatic amino acid aminotransferase II,    ARV1 protein, autophagy-specific phosphatidylinositol 3-kinase    complex protein subunit, b0017-protein, B0165-protein,    B1258-protein, B1267-protein, B1381-protein, b1933-protein,    b2165-protein, b2238-protein, b2431-protein, B2646-protein,    b2766-protein, b3120-protein, carnitine acetyltransferase, cell wall    endo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex    protein, cholinephosphate cytidylyltransferase, chorismate mutase    T/prephenate dehydrogenase (bifunctional), clathrin associated    protein complex small subunit, component of the RAM signaling    network, cysteine transporter, cytochrome c oxidase subunit VIII,    cytosolic catalase, cytosolic serine hydroxymethyltransferase,    dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,    exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest    protein, G protein coupled pheromone receptor receptor,    gamma-glutamyl kinase, glucoamylase, glycerol-3-phosphate    transporter subunit, glycine decarboxylase, glycosyltransferase,    golgi membrane exchange factor subunit, golgi membrane protein,    GPI-anchored cell wall protein, GTP-binding protein,    helix-loop-helix transcription activator that binds    inositol/choline-responsive elements, hexose transporter, histidine    kinase osmosensor that regulates an osmosensing MAP kinase cascade,    hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrier    protein dehydratase, inheritance of peroxisomes protein, integral    membrane protein localized to late Golgi vesicles, iron sulfur    cluster assembly protein, isomerase, lysine/arginine/ornithine    transporter subunit, lysine-specific metalloprotease,    lysophospholipase, Mcm1p binding transcriptional repressor, Meiotic    recombination protein, membrane protein, metal ion transporter,    microsomal beta-keto-reductase, mitochondrial intermembrane space    protein, mitochondrial protein, mitochondrial ribosomal protein of    the large subunit, mitochondrial ribosomal protein of the small    subunit, mitochondrial seryl-tRNA synthetase, molybdopterin    biosynthesis protein, myo-inositol transporter, non-essential    kinetochore protein, non-essential Ras guanine nucleotide exchange    factor, non-essential small GTPase of the Rho/Rac subfamily of    Ras-like proteins, Nuclear cap-binding protein complex subunit,    nuclear fusion protein precursor, nuclear pore complex subunit,    origin recognition complex subunit, outer membrane usher protein,    oxidoreductase, peptide transporter, peptidyl-prolyl cis-trans    isomerase, PhoH-like protein, phosphatidylserine decarboxylase,    phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteine    decarboxylase, Phosphoribosylaminoimidazole carboxylase,    potassium:hydrogen antiporter, proline dehydrogenase, protein    component of the large ribosomal subunit, protein involved in shmoo    formation and bipolar bud site selection, protein involved in    sphingolipid biosynthesis, protein kinase, protein necessary for    structural stability of L-A double-stranded RNA-containing    particles, protein required for maturation of ribosomal RNAs,    protein translocase protein, Regulatory CAT8 protein, regulatory    subunit of Glc7p type 1 protein serine-threonine phosphatase,    regulatory subunit of the 26S proteasome, repressor of G1    transcription, Rho GDP-dissociation inhibitor, ribonucleoprotein,    ribosomal protein of the small subunit, RNA polymerase III subunit,    saccharopine dehydrogenase, short chain fatty acid transporter,    signal recognition particle subunit (SRP54), signal transducing MEK    kinase, SM complex B protein for mRNA splicing, spindle checkpoint    complex subunit, splicing factor, Stationary phase protein, subunit    of cytoplasmic phenylalanyl-tRNA synthetase, subunit of the    transport protein particle (TRAPP) complex of the cis-Golgi,    threonine ammonia-lyase, transcription elongation factor,    transcription factor, Transcriptional activator, translational    elongation factor EF-3 (HEF3), transmembrane protein with a role in    cell wall polymer composition, transport protein, ubiquitin    regulatory protein, UDP-N-acetyl-glucosamine-1-P transferase,    v-SNARE binding protein, v-SNARE protein involved in Golgi    transport, xylitol dehydrogenase, yal019w-protein, ybr262c-protein,    YDR070C-protein, ydr355c-protein, YFR007W-protein,    ygr122c-a-protein, ygr266w-protein, ygr290w-protein,    YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,    yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,    YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,    yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,    ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,    ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,    yml128c-protein, YMR082C-protein, YMR126c membrane protein,    YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,    YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein,    Zinc finger protein, and zinc metalloprotease and conferring an    increased yield, especially an enhanced NUE and/or increased biomass    production, as compared to a corresponding non-transformed wild type    plant cell, plant or part thereof;-   (h) increasing the expression of the endogenous gene encoding the    polypeptide of the invention or its homologs by adding positive    expression or removing negative expression elements, e.g. homologous    recombination can be used to either introduce positive regulatory    elements like for plants the 35S enhancer into the promoter or to    remove repressor elements form regulatory regions. Further gene    conversion methods can be used to disrupt repressor elements or to    enhance to activity of positive elements-positive elements can be    randomly introduced in plants by T-DNA or transposon mutagenesis and    lines can be identified in which the positive elements have been    integrated near to a gene of the invention, the expression of which    is thereby enhanced;    and/or-   (i) modulating growth conditions of the plant in such a manner, that    the expression or activity of the gene encoding the protein of the    invention or the protein itself is enhanced;-   (j) selecting of organisms with especially high activity of the    proteins of the invention from natural or from mutagenized resources    and breeding them into the target organisms, e.g. the elite crops.

Preferably, said mRNA is the nucleic acid molecule of the presentinvention and/or the protein conferring the increased expression of aprotein encoded by the nucleic acid molecule of the present inventionalone or linked to a transit nucleic acid sequence or transit peptideencoding nucleic acid sequence or the polypeptide having the hereinmentioned activity, e.g. conferring an increased yield, especially anenhanced NUE and/or increased biomass production, as compared to acorresponding non-transformed wild type plant cell, plant or partthereof after increasing the expression or activity of the encodedpolypeptide or having the activity of a polypeptide having an activityas the protein as shown in table II column 3 or its homologs.

In general, the amount of mRNA or polypeptide in a cell or a compartmentof an organism correlates with the amount of encoded protein and thuswith the overall activity of the encoded protein in said volume. Saidcorrelation is not always linear, the activity in the volume isdependent on the stability of the molecules or the presence ofactivating or inhibiting co-factors. Further, product and eductinhibitions of enzymes are well known and described in textbooks, e.g.Stryer, Biochemistry.

In general, the amount of mRNA, polynucleotide or nucleic acid moleculein a cell or a compartment of an organism correlates with the amount ofencoded protein and thus with the overall activity of the encodedprotein in said volume. Said correlation is not always linear, theactivity in the volume is dependent on the stability of the molecules,the degradation of the molecules or the presence of activating orinhibiting co-factors. Further, product and educt inhibitions of enzymesare well known, e.g. Zinser et al. “Enzyminhibitoren”/Enzymeinhibitors”.

The activity of the abovementioned proteins and/or polypeptides encodedby the nucleic acid molecule of the present invention can be increasedin various ways. For example, the activity in an organism or in a partthereof, like a cell, is increased via increasing the gene productnumber, e.g. by increasing the expression rate, like introducing astronger promoter, or by increasing the stability of the mRNA expressed,thus increasing the translation rate, and/or increasing the stability ofthe gene product, thus reducing the proteins decayed. Further, theactivity or turnover of enzymes can be influenced in such a way that areduction or increase of the reaction rate or a modification (reductionor increase) of the affinity to the substrate results, is reached. Amutation in the catalytic center of an polypeptide of the invention,e.g. as enzyme, can modulate the turn over rate of the enzyme, e.g. aknock out of an essential amino acid can lead to a reduced or completelyknock out activity of the enzyme, or the deletion or mutation ofregulator binding sites can reduce a negative regulation like a feedbackinhibition (or a substrate inhibition, if the substrate level is alsoincreased). The specific activity of an enzyme of the present inventioncan be increased such that the turn over rate is increased or thebinding of a co-factor is improved. Improving the stability of theencoding mRNA or the protein can also increase the activity of a geneproduct. The stimulation of the activity is also under the scope of theterm “increased activity”.

Moreover, the regulation of the abovementioned nucleic acid sequencesmay be modified so that gene expression is increased. This can beachieved advantageously by means of heterologous regulatory sequences orby modifying, for example mutating, the natural regulatory sequenceswhich are present. The advantageous methods may also be combined witheach other.

In general, an activity of a gene product in an organism or partthereof, in particular in a plant cell or organelle of a plant cell, aplant, or a plant tissue or a part thereof or in a microorganism can beincreased by increasing the amount of the specific encoding mRNA or thecorresponding protein in said organism or part thereof.

“Amount of protein or mRNA” is understood as meaning the molecule numberof polypeptides or mRNA molecules in an organism, especially a plant, atissue, a cell or a cell compartment. “Increase” in the amount of aprotein means the quantitative increase of the molecule number of saidprotein in an organism, especially a plant, a tissue, a cell or a cellcompartment such as an organelle like a plastid or mitochondria or partthereof—for example by one of the methods described herein below—incomparison to a wild type, control or reference.

The increase in molecule number amounts preferably to at least 1%,preferably to more than 10%, more preferably to 30% or more, especiallypreferably to 50%, 70% or more, very especially preferably to 100%, mostpreferably to 500% or more. However, a de novo expression is alsoregarded as subject of the present invention.

A modification, i.e. an increase, can be caused by endogenous orexogenous factors. For example, an increase in activity in an organismor a part thereof can be caused by adding a gene product or a precursoror an activator or an agonist to the media or nutrition or can be causedby introducing said subjects into an organism, transient or stable.Furthermore such an increase can be reached by the introduction of theinventive nucleic acid sequence or the encoded protein in the correctcell compartment for example into the nucleus or cytoplasm respectivelyor into plastids either by transformation and/or targeting.

In one embodiment the increased yield level, especially the enhancementof the NUE and/or increased biomass production, as compared to acorresponding non-transformed wild type plant cell in the plant or apart thereof, e.g. in a cell, a tissue, a organ, an organelle, thecytosol etc., is achieved by increasing the endogenous level of thepolypeptide of the invention. Accordingly, in an embodiment of thepresent invention, the present invention relates to a process whereinthe gene copy number of a gene encoding the polynucleotide or nucleicacid molecule of the invention is increased. Further, the endogenouslevel of the polypeptide of the invention can for example be increasedby modifying the transcriptional or translational regulation of thepolypeptide.

In one embodiment an increased yield, especially the enhanced NUE and/orincreased biomass production, of the plant or part thereof can bealtered by targeted or random mutagenesis of the endogenous genes of theinvention. For example homologous recombination can be used to eitherintroduce positive regulatory elements like for plants the ³⁵S enhancerinto the promoter or to remove repressor elements form regulatoryregions. In addition gene conversion like methods described byKochevenko and Willmitzer (Plant Physiol. 132 (1), 174 (2003)) andcitations therein can be used to disrupt repressor elements or toenhance to activity of positive regulatory elements.

Furthermore positive elements can be randomly introduced in (plant)genomes by T-DNA or transposon mutagenesis and lines can be screenedfor, in which the positive elements have been integrated near to a geneof the invention, the expression of which is thereby enhanced. Theactivation of plant genes by random integrations of enhancer elementshas been described by Hayashi et al. (Science 258,1350 (1992)) or Weigelet al. (Plant Physiol. 122, 1003 (2000)) and others citied therein.

Reverse genetic strategies to identify insertions (which eventuallycarrying the activation elements) near in genes of interest have beendescribed for various cases e.g. Krysan et al. (Plant Cell 11, 2283(1999)); Sessions et al. (Plant Cell 14, 2985 (2002)); Young et al.(Plant Physiol. 125, 513 (2001)); Koprek et al. (Plant J. 24, 253(2000)); Jeon et al. (Plant J. 22, 561 (2000)); Tissier et al. (PlantCell 11, 1841 (1999)); Speulmann et al. (Plant Cell 11, 1853 (1999)).Briefly material from all plants of a large T-DNA or transposonmutagenized plant population is harvested and genomic DNA prepared. Thenthe genomic DNA is pooled following specific architectures as describedfor example in Krysan et al. (Plant Cell 11, 2283 (1999)). Pools ofgenomics DNAs are then screened by specific multiplex PCR reactionsdetecting the combination of the insertional mutagen (e.g. T-DNA orTransposon) and the gene of interest. Therefore PCR reactions are run onthe DNA pools with specific combinations of T-DNA or transposon borderprimers and gene specific primers. General rules for primer design canagain be taken from Krysan et al. (Plant Cell 11, 2283 (1999)).Rescreening of lower levels DNA pools lead to the identification ofindividual plants in which the gene of interest is activated by theinsertional mutagen.

The enhancement of positive regulatory elements or the disruption orweakening of negative regulatory elements can also be achieved throughcommon mutagenesis techniques: The production of chemically or radiationmutated populations is a common technique and known to the skilledworker. Methods for plants are described by Koorneef et al. (Mutat Res.March 93 (1) (1982)) and the citations therein and by Lightner andCaspar in “Methods in Molecular Biology” Vol. 82. These techniquesusually induce point mutations that can be identified in any known geneusing methods such as TILLING (Colbert et al., Plant Physiol, 126,(2001)).

Accordingly, the expression level can be increased if the endogenousgenes encoding a polypeptide conferring an increased expression of thepolypeptide of the present invention, in particular genes comprising thenucleic acid molecule of the present invention, are modified viahomologous recombination, Tilling approaches or gene conversion. It alsopossible to add as mentioned herein targeting sequences to the inventivenucleic acid sequences.

Regulatory sequences, if desired, in addition to a target sequence orpart thereof can be operatively linked to the coding region of anendogenous protein and control its transcription and translation or thestability or decay of the encoding mRNA or the expressed protein. Inorder to modify and control the expression, promoter, UTRs, splicingsites, processing signals, polyadenylation sites, terminators,enhancers, repressors, post transcriptional or posttranslationalmodification sites can be changed, added or amended. For example, theactivation of plant genes by random integrations of enhancer elementshas been described by Hayashi et al. (Science 258, 1350 (1992)) orWeigel et al. (Plant Physiol. 122, 1003 (2000)) and others citiedtherein. For example, the expression level of the endogenous protein canbe modulated by replacing the endogenous promoter with a strongertransgenic promoter or by replacing the endogenous 3′UTR with a 3′UTR,which provides more stability without amending the coding region.Further, the transcriptional regulation can be modulated by introductionof an artificial transcription factor as described in the examples.Alternative promoters, terminators and UTR are described below.

The activation of an endogenous polypeptide having above-mentionedactivity, e.g. having the activity of a protein as shown in table II,application no. 1, column 3 or of the polypeptide of the invention, e.g.conferring the increased yield effect, especially the enhancement of NUEand/or increased biomass production, as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof afterincrease of expression or activity in the cytosol and/or in an organellelike a plastid, can also be increased by introducing a synthetictranscription factor, which binds close to the coding region of the geneencoding the protein as shown in table II, application no. 1, column 3and activates its transcription. A chimeric zinc finger protein can beconstructed, which comprises a specific DNA-binding domain and anactivation domain as e.g. the VP16 domain of Herpes Simplex virus. Thespecific binding domain can bind to the regulatory region of the geneencoding the protein as shown in table II, application no. 1, column 3.The expression of the chimeric transcription factor in a organism, inparticular in a plant, leads to a specific expression of the protein asshown in table II, application no. 1, column 3. The methods thereto aknown to a skilled person and/or disclosed e.g. in WO01/52620, Oriz,Proc. Natl. Acad. Sci. USA, 99, 13290 (2002) or Guan, Proc. Natl. Acad.Sci. USA 99, 13296 (2002).

In one further embodiment of the process according to the invention,organisms are used in which one of the abovementioned genes, or one ofthe above-mentioned nucleic acids, is mutated in a way that the activityof the encoded gene products is less influenced by cellular factors, ornot at all, in comparison with the unmutated proteins. For example, wellknown regulation mechanism of enzymatic activity are substrateinhibition or feed back regulation mechanisms. Ways and techniques forthe introduction of substitution, deletions and additions of one or morebases, nucleotides or amino acids of a corresponding sequence aredescribed herein below in the corresponding paragraphs and thereferences listed there, e.g. in Sambrook et al., Molecular Cloning,Cold Spring Habour, N.Y., 1989. The person skilled in the art will beable to identify regulation domains and binding sites of regulators bycomparing the sequence of the nucleic acid molecule of the presentinvention or the expression product thereof with the state of the art bycomputer software means which comprise algorithms for the identifying ofbinding sites and regulation domains or by introducing into a nucleicacid molecule or in a protein systematically mutations and assaying forthose mutations which will lead to an increased specific activity or anincreased activity per volume, in particular per cell.

It can therefore be advantageous to express in an organism a nucleicacid molecule of the invention or a polypeptide of the invention derivedfrom a evolutionary distantly related organism, as e.g. using aprokaryotic gene in a eukaryotic host, as in these cases the regulationmechanism of the host cell may not weaken the activity (cellular orspecific) of the gene or its expression product.

The mutation is introduced in such a way that the enhanced yield,particularly due to one or more improved yield related traits as definedabove, especially the enhanced NUE and/or biomass increase, are notadversely affected.

Less influence on the regulation of a gene or its gene product isunderstood as meaning a reduced regulation of the enzymatic activityleading to an increased specific or cellular activity of the gene or itsproduct. An increase of the enzymatic activity is understood as meaningan enzymatic activity, which is increased by at least 10%,advantageously at least 20, 30 or 40%, especially advantageously by atleast 50, 60 or 70% in comparison with the starting organism. This leadsto an enhanced NUE and/or increased biomass production as compared to acorresponding non-transformed wild type plant cell, plant or partthereof.

The invention provides that the above methods can be performed such thatthe tolerance to abiotic environmental stress is increased, whereinparticularly the tolerance to low temperature and/or water useefficiency is increased. In another preferred embodiment the inventionprovides that the above methods can be performed such that the nutrientuse efficiency, particularly the NUE is increased. In a furtherpreferred embodiment the invention provides that the above methods canbe performed such that the tolerance to abiotic stress, particularly thetolerance to low temperature and/or water use efficiency, and at thesame time, the nutrient use efficiency, particularly the nitrogen useefficiency is increased. In another preferred embodiment the inventionprovides that the above methods can be performed such that the yield isincreased in the absence of nutrient deficiencies as well as the absenceof stress conditions. In a further preferred embodiment the inventionprovides that the above methods can be performed such that the nutrientuse efficiency, particularly the nitrogen use efficiency, and the yield,in the absence of nutrient deficiencies as well as the absence of stressconditions, is increased. In a further preferred embodiment theinvention provides that the above methods can be performed such that thetolerance to abiotic stress, particularly the tolerance to lowtemperature and/or water use efficiency, and at the same time, thenutrient use efficiency, particularly the nitrogen use efficiency, andthe yield in the absence of nutrient deficiencies as well as the absenceof stress conditions, is increased.

The invention is not limited to specific nucleic acids, specificpolypeptides, specific cell types, specific host cells, specificconditions or specific methods etc. as such, but may vary and numerousmodifications and variations therein will be apparent to those skilledin the art. It is also to be understood that the terminology used hereinis for the purpose of describing specific embodiments only and is notintended to be limiting.

The present invention also relates to isolated nucleic acids comprisinga nucleic acid molecule selected from the group consisting of:

-   (a) a nucleic acid molecule encoding the polypeptide shown in column    7 of table II B, application no. 1;-   (b) a nucleic acid molecule shown in column 7 of table I B,    application no. 1;-   (c) a nucleic acid molecule, which, as a result of the degeneracy of    the genetic code, can be derived from a polypeptide sequence    depicted in column 5 or 7 of table II, application no. 1, and    confers an increased yield, especially an enhanced NUE and/or    increased biomass production, as compared to a corresponding    non-transformed wild type plant cell, a plant or a part thereof;-   (d) a nucleic acid molecule having at least 30% identity, preferably    at least 40%, 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%,    99%, 99.5%, with the nucleic acid molecule sequence of a    polynucleotide comprising the nucleic acid molecule shown in column    5 or 7 of table I, application no. 1, and confers an increased    yield, especially an enhanced NUE and/or increased biomass    production, as compared to a corresponding non-transformed wild type    plant cell, a plant or a part thereof;-   (e) a nucleic acid molecule encoding a polypeptide having at least    30% identity, preferably at least 40%, 50%, 60%, 70%, 75%, 80%, 85%,    90%, 95%, 96%, 97%, 98%, 99%, 99.5%, with the amino acid sequence of    the polypeptide encoded by the nucleic acid molecule of (a),    (b), (c) or (d) and having the activity represented by a nucleic    acid molecule comprising a polynucleotide as depicted in column 5 of    table I, application no. 1, and confers an increased yield,    especially an enhanced NUE and/or increased biomass production, as    compared to a corresponding non-transformed wild type plant cell, a    plant or a part thereof;-   (f) nucleic acid molecule which hybridizes with a nucleic acid    molecule of (a), (b), (c), (d) or (e) under stringent hybridization    conditions and confers an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, a plant or a    part thereof;-   (g) a nucleic acid molecule encoding a polypeptide which can be    isolated with the aid of monoclonal or polyclonal antibodies made    against a polypeptide encoded by one of the nucleic acid molecules    of (a), (b), (c), (d), (e) or (f) and having the activity    represented by the nucleic acid molecule comprising a polynucleotide    as depicted in column 5 of table I, application no. 1;-   (h) a nucleic acid molecule encoding a polypeptide comprising the    consensus sequence or one or more polypeptide motifs as shown in    column 7 of table IV, application no. 1, and preferably having the    activity represented by a protein molecule comprising a polypeptide    as depicted in column 5 of table II or IV, application no. 1,-   (i) a nucleic acid molecule encoding a polypeptide having the    activity represented by a protein as depicted in column 5 of table    II, application no. 1, and confers an increased yield, especially an    enhanced NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, a plant or a    part thereof;-   (i) nucleic acid molecule which comprises a polynucleotide, which is    obtained by amplifying a cDNA library or a genomic library using the    primers in column 7 of table III, application no. 1, (which in a    special embodiment do not start at their 5′-end with the nucleotides    ATA and) preferably having the activity represented by a protein    molecule comprising a polypeptide as depicted in column 5 of table    II or IV, application no. 1;    and-   (k) a nucleic acid molecule which is obtainable by screening a    suitable nucleic acid library, especially a cDNA library and/or a    genomic library, under stringent hybridization conditions with a    probe comprising a complementary sequence of a nucleic acid molecule    of (a) or (b) or with a fragment thereof, having at least 15 nt,    preferably 20 nt, 30 nt, 50 nt, 100 nt, 200 nt, 500 nt, 750 nt or    1000 nt of a nucleic acid molecule complementary to a nucleic acid    molecule sequence characterized in (a) to (e) and encoding a    polypeptide having the activity represented by a protein comprising    a polypeptide as depicted in column 5 of table II, application no.    1;    whereby the nucleic acid molecule according to (a), (b), (c), (d),    (e), (f), (g), (h), (i), (j) and (k) is at least in one or more    nucleotides different from the sequence depicted in column 5 or 7 of    table I A, application no. 1, and preferably which encodes a protein    which differs at least in one or more amino acids from the protein    sequences depicted in column 5 or 7 of table II A, application no.    1.

In one embodiment the invention relates to homologs of theafore-mentioned sequences, which can be isolated advantageously fromyeast, fungi, viruses, algae, bacteria, such as Acetobacter (subgen.Acetobacter) aceti; Acidithiobacillus ferrooxidans; Acinetobacter sp.;Actinobacillus sp; Aeromonas salmonicida; Agrobacterium tumefaciens;Aquifex aeolicus; Arcanobacterium pyogenes; Aster yellows phytoplasma;Bacillus sp.; Bifidobacterium sp.; Borrelia burgdorferi; Brevibacteriumlinens; Brucella melitensis; Buchnera sp.; Butyrivibrio fibrisolvens;Campylobacter jejuni; Caulobacter crescentus; Chlamydia sp.;Chlamydophila sp.; Chlorobium limicola; Citrobacter rodentium;Clostridium sp.; Comamonas testosteroni; Corynebacterium sp.; Coxiellaburnetii; Deinococcus radiodurans; Dichelobacter nodosus; Edwardsiellaictaluri; Enterobacter sp.; Erysipelothrix rhusiopathiae; Escherichiacoli; Flavobacterium sp.; Francisella tularensis; Frankia sp. Cpl1;Fusobacterium nucleatum; Geobacillus stearothermophilus; Gluconobacteroxydans; Haemophilus sp.; Helicobacter pylori; Klebsiella pneumoniae;Lactobacillus sp.; Lactococcus lactis; Listeria sp.; Mannheimiahaemolytica; Mesorhizobium loti; Methylophaga thalassica; Microcystisaeruginosa; Microscilla sp. PRE1; Moraxella sp. TA144; Mycobacteriumsp.; Mycoplasma sp.; Neisseria sp.; Nitrosomonas sp.; Nostoc sp. PCC7120; Novosphingobium aromaticivorans; Oenococcus oeni; Pantoea citrea;Pasteurella multocida; Pediococcus pentosaceus; Phormidium foveolarum;Phytoplasma sp.; Plectonema boryanum; Prevotella ruminicola;Propionibacterium sp.; Proteus vulgaris; Pseudomonas sp.; Ralstonia sp.;Rhizobium sp.; Rhodococcus equi; Rhodothermus marinus; Rickettsia sp.;Riemerella anatipestifer; Ruminococcus flavefaciens; Salmonella sp.;Selenomonas ruminantium; Serratia entomophila; Shigella sp.;Sinorhizobium meliloti; Staphylococcus sp.; Streptococcus sp.;Streptomyces sp.; Synechococcus sp.; Synechocystis sp. PCC 6803;Thermotoga maritima; Treponema sp.; Ureaplasma urealyticum; Vibriocholerae; Vibrio parahaemolyticus; Xylella fastidiosa; Yersinia sp.;Zymomonas mobilis, preferably Salmonella sp. or Escherichia coli orplants, preferably from yeasts such as from the genera Saccharomyces,Pichia, Candida, Hansenula, Torulopsis or Schizosaccharomyces or plantssuch as Arabidopsis thaliana, maize, wheat, rye, oat, triticale, rice,barley, soybean, peanut, cotton, borage, sunflower, linseed, primrose,rapeseed, canola and turnip rape, manihot, pepper, sunflower, tagetes,solanaceous plant such as potato, tobacco, eggplant and tomato, Viciaspecies, pea, alfalfa, bushy plants such as coffee, cacao, tea, Salixspecies, trees such as oil palm, coconut, perennial grass, such asryegrass and fescue, and forage crops, such as alfalfa and clover andfrom spruce, pine or fir for example. More preferably homologs ofaforementioned sequences can be isolated from Saccharomyces cerevisiae,E. coli or Synechocystis sp. or plants, preferably Brassica napus,Glycine max, Zea mays, cotton or Oryza sativa.

The (NUE related) proteins (NUERPs) of the present invention arepreferably produced by recombinant DNA techniques. For example, anucleic acid molecule encoding the protein is cloned into an expressionvector, for example in to a binary vector, the expression vector isintroduced into a host cell, for example the Arabidopsis thaliana wildtype NASC N906 or any other plant cell as described in the examples seebelow, and the NUE related protein is expressed in said host cell.Examples for binary vectors are pBIN19, pBI101, pBinAR, pGPTV, pCAMBIA,pBIB-HYG, pBecks, pGreen or pPZP (Hajukiewicz, P. et al., Plant Mol.Biol. 25, 989 (1994), and Hellens et al, Trends in Plant Science 5, 446(2000)).

In one embodiment the (NUE related) protein (NUERP) of the presentinvention is preferably produced in a compartment of the cell, morepreferably in the plastids. Ways of introducing nucleic acids intoplastids and producing proteins in this compartment are known to theperson skilled in the art have been also described in this application.

In another embodiment of the (NUE related) protein (NUERP) of thepresent invention is preferably produced in the cytosol of the cell.Ways of producing proteins in the cytosol are known to the personskilled in the art.

In another embodiment the protein of the present invention is preferablyproduced cytoplasmic, meaning without artificial targeting as defined in0066.1.1.1. Ways of producing proteins without artificial targeting areknown to the person skilled in the art.

Advantageously, the nucleic acid sequences according to the invention orthe gene construct together with at least one reporter gene are clonedinto an expression cassette, which is introduced into the organism via avector or directly into the genome. This reporter gene should allow easydetection via a growth, fluorescence, chemical, bioluminescence orresistance assay or via a photometric measurement. Examples of reportergenes which may be mentioned are antibiotic- or herbicide-resistancegenes, hydrolase genes, fluorescence protein genes, bioluminescencegenes, sugar or nucleotide metabolic genes or biosynthesis genes such asthe Ura3 gene, the IIv2 gene, the luciferase gene, the β-galactosidasegene, the gfp gene, the 2-desoxyglucose-6-phosphate phosphatase gene,the β-glucuronidase gene, β-lactamase gene, the neomycinphosphotransferase gene, the hygromycin phosphotransferase gene, amutated acetohydroxyacid synthase (AHAS) gene (also known asacetolactate synthase (ALS) gene), a gene for a D-amino acidmetabolizing enzmye or the BASTA (=gluphosinate-resistance) gene. Thesegenes permit easy measurement and quantification of the transcriptionactivity and hence of the expression of the genes. In this way genomepositions may be identified which exhibit differing productivity.

In a preferred embodiment a nucleic acid construct, for example anexpression cassette, comprises upstream, i.e. at the 5′ end of theencoding sequence, a promoter and downstream, i.e. at the 3′ end, apolyadenylation signal and optionally other regulatory elements whichare operably linked to the intervening encoding sequence with one of thenucleic acids of SEQ ID NO as depicted in table I, application no. 1,column 5 and 7. By an operable linkage is meant the sequentialarrangement of promoter, encoding sequence, terminator and optionallyother regulatory elements in such a way that each of the regulatoryelements can fulfill its function in the expression of the encodingsequence in due manner. In one embodiment the sequences preferred foroperable linkage are targeting sequences for ensuring subcellularlocalization in plastids. However, targeting sequences for ensuringsubcellular localization in the mitochondrium, in the endoplasmicreticulum (=ER), in the nucleus, in oil corpuscles or other compartmentsmay also be employed as well as translation promoters such as the 5′lead sequence in tobacco mosaic virus (Gallie et al., Nucl. Acids Res.15 8693 (1987)).

A nucleic acid construct, for example an expression cassette may, forexample, contain a constitutive promoter or a tissue-specific promoter(preferably the USP or napin promoter) the gene to be expressed and theER retention signal. For the ER retention signal the KDEL amino acidsequence (lysine, aspartic acid, glutamic acid, leucine) or the KKXamino acid sequence (lysine-lysine-X-stop, wherein X means every otherknown amino acid) is preferably employed.

For expression in a host organism, for example a plant, the expressioncassette is advantageously inserted into a vector such as by way ofexample a plasmid, a phage or other DNA which allows optimal expressionof the genes in the host organism. Examples of suitable plasmids are: inE. coli pLG338, pACYC184, pBR series such as e.g. pBR322, pUC seriessuch as pUC18 or pUC19, M113mp series, pKC30, pRep4, pHS1, pHS2,pPLc236, pMBL24, pLG200, pUR290, pIN-III¹¹³-B1, λgt11 or pBdCI; inStreptomyces pIJ101, pIJ364, pIJ702 or pIJ361; in Bacillus pUB110, pC194or pBD214; in Corynebacterium pSA77 or pAJ667; in fungi pALS1, pIL2 orpBB116; other advantageous fungal vectors are described by Romanos M. A.et al., Yeast 8, 423 (1992) and by van den Hondel, C.A.M.J. J. et al.[(1991) “Heterologous gene expression in filamentous fungi”] as well asin “More Gene Manipulations” in “Fungi” in Bennet J.W. & Lasure L. L.,eds., pp. 396-428, Academic Press, San Diego, and in “Gene transfersystems and vector development for filamentous fungi” [van den Hondel,C.A.M.J.J. & Punt, P.J. (1991) in: Applied Molecular Genetics of Fungi,Peberdy, J. F. et al., eds., pp. 1-28, Cambridge University Press:Cambridge]. Examples of advantageous yeast promoters are 2 μM, pAG-1,YEp6, YEp13 or pEMBLYe23. Examples of algal or plant promoters arepLGV23, pGHlac⁺, pBIN19, pAK2004, pVKH or pDH51 (see Schmidt, R. andWillmitzer, L., Plant Cell Rep. 7, 583 (1988))). The vectors identifiedabove or derivatives of the vectors identified above are a smallselection of the possible plasmids. Further plasmids are well known tothose skilled in the art and may be found, for example, in “CloningVectors” (Eds. Pouwels P. H. et al. Elsevier, Amsterdam-New York-Oxford,1985, ISBN 0 444 904018). Suitable plant vectors are described interalia in “Methods in Plant Molecular Biology and Biotechnology” (CRCPress, Ch. 6/7, pp. 71-119). Advantageous vectors are known as shuttlevectors or binary vectors which replicate in E. coli and Agrobacterium.

By vectors is meant with the exception of plasmids all other vectorsknown to those skilled in the art such as by way of example phages,viruses such as SV40, CMV, baculovirus, adenovirus, transposons, ISelements, phasmids, phagemids, cosmids, linear or circular DNA. Thesevectors can be replicated autonomously in the host organism or bechromosomally replicated, chromosomal replication being preferred.

In a further embodiment of the vector the expression cassette accordingto the invention may also advantageously be introduced into theorganisms in the form of a linear DNA and be integrated into the genomeof the host organism by way of heterologous or homologous recombination.This linear DNA may be composed of a linearized plasmid or only of theexpression cassette as vector or the nucleic acid sequences according tothe invention.

In a further advantageous embodiment the nucleic acid sequence accordingto the invention can also be introduced into an organism on its own.

If in addition to the nucleic acid sequence according to the inventionfurther genes are to be introduced into the organism, all together witha reporter gene in a single vector or each single gene with a reportergene in a vector in each case can be introduced into the organism,whereby the different vectors can be introduced simultaneously orsuccessively.

The vector advantageously contains at least one copy of the nucleic acidsequences according to the invention and/or the expression cassette(=gene construct) according to the invention.

The invention further provides an isolated recombinant expression vectorcomprising a nucleic acid encoding a polypeptide as depicted in tableII, application no. 1, column 5 or 7, wherein expression of the vectorin a host cell results in increased yield, especially in enhanced NUEand/or biomass production, as compared to a wild type variety of thehost cell.

As used herein, the term “vector” refers to a nucleic acid moleculecapable of transporting another nucleic acid to which it has beenlinked. One type of vector is a “plasmid”, which refers to a circulardouble stranded DNA loop into which additional DNA segments can beligated. Another type of vector is a viral vector, wherein additionalDNA segments can be ligated into the viral genome. Certain vectors arecapable of autonomous replication in a host cell into which they areintroduced (e.g. bacterial vectors having a bacterial origin ofreplication and episomal mammalian vectors). Other vectors (e.g.non-episomal mammalian vectors) are integrated into the genome of a hostcell or an organelle upon introduction into the host cell, and therebyare replicated along with the host or organelle genome. Moreover,certain vectors are capable of directing the expression of genes towhich they are operatively linked. Such vectors are referred to hereinas “expression vectors.” In general, expression vectors of utility inrecombinant DNA techniques are often in the form of plasmids. In thepresent specification, “plasmid” and “vector” can be usedinterchangeably as the plasmid is the most commonly used form of vector.However, the invention is intended to include such other forms ofexpression vectors, such as viral vectors (e.g., replication defectiveretroviruses, adenoviruses, and adeno-associated viruses), which serveequivalent functions.

The recombinant expression vectors of the invention comprise a nucleicacid of the invention in a form suitable for expression of the nucleicacid in a host cell, which means that the recombinant expression vectorsinclude one or more regulatory sequences, selected on the basis of thehost cells to be used for expression, which is operatively linked to thenucleic acid sequence to be expressed. As used herein with respect to arecombinant expression vector, “operatively linked” is intended to meanthat the nucleotide sequence of interest is linked to the regulatorysequence(s) in a manner which allows for expression of the nucleotidesequence (e.g. in an in vitro transcription/translation system or in ahost cell when the vector is introduced into the host cell). The term“regulatory sequence” is intended to include promoters, enhancers, andother expression control elements (e.g. polyadenylation signals). Suchregulatory sequences are described, for example, in Goeddel, GeneExpression Technology: Methods in Enzymology 185, Academic Press, SanDiego, Calif. (1990), and Gruber and Crosby, in: Methods in PlantMolecular Biology and Biotechnology, eds. Glick and Thompson, Chapter 7,89-108, CRC Press; Boca Raton, Fla., including the references therein.Regulatory sequences include those that direct constitutive expressionof a nucleotide sequence in many types of host cells and those thatdirect expression of the nucleotide sequence only in certain host cellsor under certain conditions. It will be appreciated by those skilled inthe art that the design of the expression vector can depend on suchfactors as the choice of the host cell to be transformed, the level ofexpression of polypeptide desired, etc. The expression vectors of theinvention can be introduced into host cells to thereby producepolypeptides or peptides, including fusion polypeptides or peptides,encoded by nucleic acids as described herein (e.g., NUERPs, mutant formsof NUERPs, fusion polypeptides, etc.).

The recombinant expression vectors of the invention can be designed forexpression of the polypeptide of the invention in plant cells. Forexample, NUERP genes can be expressed in plant cells (see Schmidt R.,and Willmitzer L., Plant Cell Rep. 7 (1988); Plant Molecular Biology andBiotechnology, C Press, Boca Raton, Fla., Chapter 6/7, p. 71-119 (1993);White F.F., Jenes B. et al., Techniques for Gene Transfer, in:Transgenic Plants, Vol. 1, Engineering and Utilization, eds. Kung and WuR., 128-43, Academic Press: 1993; Potrykus, Annu. Rev. Plant Physiol.Plant Molec. Biol. 42, 205 (1991) and references cited therein).Suitable host cells are discussed further in Goeddel, Gene ExpressionTechnology: Methods in Enzymology 185, Academic Press: San Diego, Calif.(1990). Alternatively, the recombinant expression vector can betranscribed and translated in vitro, for example using T7 promoterregulatory sequences and T7 polymerase.

Expression of polypeptides in prokaryotes is most often carried out withvectors containing constitutive or inducible promoters directing theexpression of either fusion or non-fusion polypeptides. Fusion vectorsadd a number of amino acids to a polypeptide encoded therein, usually tothe amino terminus of the recombinant polypeptide but also to theC-terminus or fused within suitable regions in the polypeptides. Suchfusion vectors typically serve three purposes: 1) to increase expressionof a recombinant polypeptide; 2) to increase the solubility of arecombinant polypeptide; and 3) to aid in the purification of arecombinant polypeptide by acting as a ligand in affinity purification.Often, in fusion expression vectors, a proteolytic cleavage site isintroduced at the junction of the fusion moiety and the recombinantpolypeptide to enable separation of the recombinant polypeptide from thefusion moiety subsequent to purification of the fusion polypeptide. Suchenzymes, and their cognate recognition sequences, include Factor Xa,thrombin, and enterokinase.

By way of example the plant expression cassette can be installed in thepRT transformation vector ((a) Toepfer et al., Methods Enzymol. 217, 66(1993), (b) Toepfer et al., Nucl. Acids. Res. 15, 5890 (1987)).

Alternatively, a recombinant vector (=expression vector) can also betranscribed and translated in vitro, e.g. by using the T7 promoter andthe T7 RNA polymerase.

Expression vectors employed in prokaryotes frequently make use ofinducible systems with and without fusion proteins or fusionoligopeptides, wherein these fusions can ensue in both N-terminal andC-terminal manner or in other useful domains of a protein. Such fusionvectors usually have the following purposes: 1) to increase the RNAexpression rate; 2) to increase the achievable protein synthesis rate;3) to increase the solubility of the protein; 4) or to simplifypurification by means of a binding sequence usable for affinitychromatography. Proteolytic cleavage points are also frequentlyintroduced via fusion proteins, which allow cleavage of a portion of thefusion protein and purification. Such recognition sequences forproteases are recognized, e.g. factor Xa, thrombin and enterokinase.

Typical advantageous fusion and expression vectors are pGEX (PharmaciaBiotech Inc; Smith D.B. and Johnson K.S., Gene 67, 31 (1988)), pMAL (NewEngland Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.)which contains glutathione S-transferase (GST), maltose binding proteinor protein A.

In one embodiment, the coding sequence of the polypeptide of theinvention is cloned into a pGEX expression vector to create a vectorencoding a fusion polypeptide comprising, from the N-terminus to theC-terminus, GST-thrombin cleavage site-X polypeptide. The fusionpolypeptide can be purified by affinity chromatography usingglutathione-agarose resin. Recombinant PKNUERP unfused to GST can berecovered by cleavage of the fusion polypeptide with thrombin.

Other examples of E. coli expression vectors are pTrc (Amann et al.,Gene 69, 301 (1988)) and pET vectors (Studier et al., Gene ExpressionTechnology: Methods in Enzymology 185, Academic Press, San Diego, Calif.(1990) 60-89; Stratagene, Amsterdam, The Netherlands).

Target gene expression from the pTrc vector relies on host RNApolymerase transcription from a hybrid trp-lac fusion promoter. Targetgene expression from the pET 11d vector relies on transcription from aT7 gn10-lac fusion promoter mediated by a co-expressed viral RNApolymerase (T7 gn1). This viral polymerase is supplied by host strainsBL21(DE3) or HMS174(DE3) from a resident I prophage harboring a T7 gn1gene under the transcriptional control of the lacUV 5 promoter.

In a preferred embodiment of the present invention, the NUERPs areexpressed in plants and plants cells such as unicellular plant cells(e.g. algae) (see Falciatore et al., Marine Biotechnology 1 (3), 239(1999) and references therein) and plant cells from higher plants (e.g.,the spermatophytes, such as crop plants). A nucleic acid molecule codingfor NUERP as depicted in table II, application no. 1, column 5 or 7 maybe “introduced” into a plant cell by any means, including transfection,transformation or transduction, electroporation, particle bombardment,agroinfection, and the like. One transformation method known to those ofskill in the art is the dipping of a flowering plant into anAgrobacteria solution, wherein the Agrobacteria contains the nucleicacid of the invention, followed by breeding of the transformed gametes.

Other suitable methods for transforming or transfecting host cellsincluding plant cells can be found in Sambrook et al., MolecularCloning: A Laboratory Manual. 2^(nd), ed., Cold Spring HarborLaboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor,N.Y., 1989, and other laboratory manuals such as Methods in MolecularBiology, 1995, Vol. 44, Agrobacterium protocols, ed: Gartland and Davey,Humana Press, Totowa, N.J. As increased NUE and/or biomass production isa general trait wished to be inherited into a wide variety of plantslike maize, wheat, rye, oat, triticale, rice, barley, soybean, peanut,cotton, rapeseed and canola, manihot, pepper, sunflower and tagetes,solanaceous plants like potato, tobacco, eggplant, and tomato, Viciaspecies, pea, alfalfa, bushy plants (coffee, cacao, tea), Salix species,trees (oil palm, coconut), perennial grasses, and forage crops, thesecrop plants are also preferred target plants for a genetic engineeringas one further embodiment of the present invention. Forage cropsinclude, but are not limited to Wheatgrass, Canarygrass, Bromegrass,Wildrye Grass, Bluegrass, Orchardgrass, Alfalfa, Salfoin, BirdsfootTrefoil, Alsike Clover, Red Clover and Sweet Clover.

In one embodiment of the present invention, transfection of a nucleicacid molecule coding for NUERP as depicted in table II, application no.1, column 5 or 7 into a plant is achieved by Agrobacterium mediated genetransfer. Agrobacterium mediated plant transformation can be performedusing for example the GV3101(pMP90) (Koncz and Schell, Mol. Gen. Genet.204, 383 (1986)) or LBA4404 (Clontech) Agrobacterium tumefaciens strain.Transformation can be performed by standard transformation andregeneration techniques (Deblaere et al., Nucl. Acids Res. 13, 4777(1994), Gelvin, Stanton B. and Schilperoort Robert A, Plant MolecularBiology Manual, 2^(nd) Ed.—Dordrecht: Kluwer Academic Publ., 1995.—inSect., Ringbuc Zentrale Signatur: BT11-P ISBN 0-7923-2731-4; GlickBernard R., Thompson John E., Methods in Plant Molecular Biology andBiotechnology, Boca Raton: CRC Press, 1993 360 S., ISBN 0-8493-5164-2).For example, rapeseed can be transformed via cotyledon or hypocotyltransformation (Moloney et al., Plant Cell Report 8, 238 (1989); DeBlock et al., Plant Physiol. 91, 694 (1989)). Use of antibiotics forAgrobacterium and plant selection depends on the binary vector and theAgrobacterium strain used for transformation. Rapeseed selection isnormally performed using kanamycin as selectable plant marker.Agrobacterium mediated gene transfer to flax can be performed using, forexample, a technique described by Mlynarova et al., Plant Cell Report13, 282 (1994). Additionally, transformation of soybean can be performedusing for example a technique described in European Patent No. 424 047,U.S. Pat. No. 5,322,783, European Patent No. 397 687, U.S. Pat. No.5,376,543 or U.S. Pat. No. 5,169,770. Transformation of maize can beachieved by particle bombardment, polyethylene glycol mediated DNAuptake or via the silicon carbide fiber technique. (See, for example,Freeling and Walbot “The maize handbook” Springer Verlag: New York(1993) ISBN 3-540-97826-7). A specific example of maize transformationis found in U.S. Pat. No. 5,990,387, and a specific example of wheattransformation can be found in PCT Application No. WO 93/07256.

According to the present invention, the introduced nucleic acid moleculecoding for NUERP as depicted in table II, application no. 1, column 5 or7 may be maintained in the plant cell stably if it is incorporated intoa non-chromosomal autonomous replicon or integrated into the plantchromosomes or organelle genome. Alternatively, the introduced NUERP maybe present on an extra-chromosomal non-replicating vector and betransiently expressed or transiently active.

In one embodiment, a homologous recombinant microorganism can be createdwherein the NUERP is integrated into a chromosome, a vector is preparedwhich contains at least a portion of a nucleic acid molecule coding forNUERP as depicted in table II, application no. 1, column 5 or 7 intowhich a deletion, addition, or substitution has been introduced tothereby alter, e.g., functionally disrupt, the NUERP gene. Preferably,the NUERP gene is a yeast, E. coli gene, but it can be a homolog from arelated plant or even from a mammalian or insect source. The vector canbe designed such that, upon homologous recombination, the endogenousnucleic acid molecule coding for NUERP as depicted in table II,application no. 1, column 5 or 7 is mutated or otherwise altered butstill encodes a functional polypeptide (e.g., the upstream regulatoryregion can be altered to thereby alter the expression of the endogenousNUERP). In a preferred embodiment the biological activity of the proteinof the invention is increased upon homologous recombination. To create apoint mutation via homologous recombination, DNA-RNA hybrids can be usedin a technique known as chimeraplasty (Cole-Strauss et al., NucleicAcids Research 27 (5),1323 (1999) and Kmiec, Gene Therapy AmericanScientist. 87 (3), 240 (1999)). Homologous recombination procedures inPhyscomitrella patens are also well known in the art and arecontemplated for use herein.

Whereas in the homologous recombination vector, the altered portion ofthe nucleic acid molecule coding for NUERP as depicted in table II,application no. 1, column 5 or 7 is flanked at its 5′ and 3′ ends by anadditional nucleic acid molecule of the NUERP gene to allow forhomologous recombination to occur between the exogenous NUERP genecarried by the vector and an endogenous NUERP gene, in a microorganismor plant. The additional flanking NUERP nucleic acid molecule is ofsufficient length for successful homologous recombination with theendogenous gene. Typically, several hundreds of base pairs up tokilobases of flanking DNA (both at the 5′ and 3′ ends) are included inthe vector. See, e.g., Thomas K.R., and Capecchi M.R., Cell 51, 503(1987) for a description of homologous recombination vectors or Streppet al., PNAS, 95 (8), 4368 (1998) for cDNA based recombination inPhyscomitrella patens. The vector is introduced into a microorganism orplant cell (e.g. via polyethylene glycol mediated DNA), and cells inwhich the introduced NUERP gene has homologously recombined with theendogenous NUERP gene are selected using art-known techniques.

Whether present in an extra-chromosomal non-replicating vector or avector that is integrated into a chromosome, the nucleic acid moleculecoding for NUERP as depicted in table II, application no. 1, column 5 or7 preferably resides in a plant expression cassette. A plant expressioncassette preferably contains regulatory sequences capable of drivinggene expression in plant cells that are operatively linked so that eachsequence can fulfill its function, for example, termination oftranscription by polyadenylation signals. Preferred polyadenylationsignals are those originating from Agrobacterium tumefaciens t-DNA suchas the gene 3 known as octopine synthase of the Ti-plasmid pTiACH5(Gielen et al., EMBO J. 3, 835 (1984)) or functional equivalents thereofbut also all other terminators functionally active in plants aresuitable. As plant gene expression is very often not limited ontranscriptional levels, a plant expression cassette preferably containsother operatively linked sequences like translational enhancers such asthe overdrive-sequence containing the 5″-untranslated leader sequencefrom tobacco mosaic virus enhancing the polypeptide per RNA ratio(Gallie et al., Nucl. Acids Research 15, 8693 (1987)). Examples of plantexpression vectors include those detailed in: Becker D. et al., PlantMol. Biol. 20, 1195 (1992); and Bevan M.W., Nucl. Acid. Res. 12, 8711(1984); and “Vectors for Gene Transfer in Higher Plants” in: TransgenicPlants, Vol. 1, Engineering and Utilization, eds. Kung and Wu R.,Academic Press, 1993, S. 15-38.

“Transformation” is defined herein as a process for introducingheterologous DNA into a plant cell, plant tissue, or plant. It may occurunder natural or artificial conditions using various methods well knownin the art. Transformation may rely on any known method for theinsertion of foreign nucleic acid sequences into aprokaryotic oreukaryotic host cell. The method is selected based on the host cellbeing transformed and may include, but is not limited to, viralinfection, electroporation, lipofection, and particle bombardment. Such“transformed” cells include stably transformed cells in which theinserted DNA is capable of replication either as an autonomouslyreplicating plasmid or as part of the host chromosome. They also includecells which transiently express the inserted DNA or RNA for limitedperiods of time. Transformed plant cells, plant tissue, or plants areunderstood to encompass not only the end product of a transformationprocess, but also transgenic progeny thereof.

The terms “transformed,” “transgenic,” and “recombinant” refer to a hostorganism such as a bacterium or a plant into which a heterologousnucleic acid molecule has been introduced. The nucleic acid molecule canbe stably integrated into the genome of the host or the nucleic acidmolecule can also be present as an extrachromosomal molecule. Such anextrachromosomal molecule can be auto-replicating. Transformed cells,tissues, or plants are understood to encompass not only the end productof a transformation process, but also transgenic progeny thereof. A“non-transformed”, “non-transgenic” or “non-recombinant” host refers toa wild-type organism, e.g. a bacterium or plant, which does not containthe heterologous nucleic acid molecule.

A “transgenic plant”, as used herein, refers to a plant which contains aforeign nucleotide sequence inserted into either its nuclear genome ororganellar genome. It encompasses further the offspring generations i.e.the T1-, T2- and consecutively generations or BC1-, BC2- andconsecutively generation as well as crossbreeds thereof withnon-transgenic or other transgenic plants.

The host organism (=transgenic organism) advantageously contains atleast one copy of the nucleic acid according to the invention and/or ofthe nucleic acid construct according to the invention.

In principle all plants can be used as host organism. Preferredtransgenic plants are, for example, selected from the familiesAceraceae, Anacardiaceae, Apiaceae, Asteraceae, Brassicaceae, Cactaceae,Cucurbitaceae, Euphorbiaceae, Fabaceae, Malvaceae, Nymphaeaceae,Papaveraceae, Rosaceae, Salicaceae, Solanaceae, Arecaceae, Bromeliaceae,Cyperaceae, Iridaceae, Liliaceae, Orchidaceae, Gentianaceae, Labiaceae,Magnoliaceae, Ranunculaceae, Carifolaceae, Rubiaceae, Scrophulariaceae,Caryophyllaceae, Ericaceae, Polygonaceae, Violaceae, Juncaceae orPoaceae and preferably from a plant selected from the group of thefamilies Apiaceae, Asteraceae, Brassicaceae, Cucurbitaceae, Fabaceae,Papaveraceae, Rosaceae, Solanaceae, Liliaceae or Poaceae. Preferred arecrop plants such as plants advantageously selected from the group of thegenus peanut, oilseed rape, canola, sunflower, safflower, olive, sesame,hazelnut, almond, avocado, bay, pumpkin/squash, linseed, soya,pistachio, borage, maize, wheat, rye, oats, sorghum and millet,triticale, rice, barley, cassava, potato, sugarbeet, egg plant, alfalfa,and perennial grasses and forage plants, oil palm, vegetables(brassicas, root vegetables, tuber vegetables, pod vegetables, fruitingvegetables, onion vegetables, leafy vegetables and stem vegetables),buckwheat, Jerusalem artichoke, broad bean, vetches, lentil, dwarf bean,lupin, clover and Lucerne for mentioning only some of them.

In one embodiment of the invention transgenic plants are selected fromthe group comprising cereals, soybean, rapeseed (including oil seedrape, especially canola and winter oil seed rape), cotton sugarcane andpotato, especially corn, soy, rapeseed (including oil seed rape,especially canola and winter oil seed rape), cotton, wheat and rice.

In another embodiment of the invention the transgenic plant is agymnosperm plant, especially a spruce, pine or fir.

In one preferred embodiment, the host plant is selected from thefamilies Aceraceae, Anacardiaceae, Apiaceae, Asteraceae, Brassicaceae,Cactaceae, Cucurbitaceae, Euphorbiaceae, Fabaceae, Malvaceae,Nymphaeaceae, Papaveraceae, Rosaceae, Salicaceae, Solanaceae, Arecaceae,Bromeliaceae, Cyperaceae, Iridaceae, Liliaceae, Orchidaceae,Gentianaceae, Labiaceae, Magnoliaceae, Ranunculaceae, Carifolaceae,Rubiaceae, Scrophulariaceae, Caryophyllaceae, Ericaceae, Polygonaceae,Violaceae, Juncaceae or Poaceae and preferably from a plant selectedfrom the group of the families Apiaceae, Asteraceae, Brassicaceae,Cucurbitaceae, Fabaceae, Papaveraceae, Rosaceae, Solanaceae, Liliaceaeor Poaceae. Preferred are crop plants and in particular plants mentionedherein above as host plants such as the families and genera mentionedabove for example preferred the species Anacardium occidentale,Calendula officinalis, Carthamus tinctorius, Cichorium intybus, Cynarascolymus, Helianthus annus, Tagetes lucida, Tagetes erecta, Tagetestenuifolia; Daucus carota; Corylus avellana, Corylus colurna, Boragoofficinalis; Brassica napus, Brassica rapa ssp., Sinapis arvensisBrassica juncea, Brassica juncea var. juncea, Brassica juncea var.crispifolia, Brassica juncea var. foliosa, Brassica nigra, Brassicasinapioides, Melanosinapis communis, Brassica oleracea, Arabidopsisthaliana, Anana comosus, Ananas ananas, Bromelia comosa, Carica papaya,Cannabis sative, Ipomoea batatus, Ipomoea pandurata, Convolvulusbatatas, Convolvulus tilliaceus, Ipomoea fastigiata, Ipomoea tiliacea,Ipomoea triloba, Convolvulus panduratus, Beta vulgaris, Beta vulgarisvar. altissima, Beta vulgaris var. vulgaris, Beta maritima, Betavulgaris var. perennis, Beta vulgaris var. conditiva, Beta vulgaris var.esculenta, Cucurbita maxima, Cucurbita mixta, Cucurbita pepo, Cucurbitamoschata, Olea europaea, Manihot utillssima, Janipha manihot, Jatrophamanihot, Manihot aipil, Manihot dulcis, Manihot manihot, Manihotmelanobasis, Manihot esculenta, Ricinus communis, Pisum sativum, Pisumarvense, Pisum humile, Medicago sativa, Medicago falcata, Medicagovaria, Glycine max Dolichos soja, Glycine gracilis, Glycine hispida,Phaseolus max, Soja hispida, Soja max, Cocos nucifera, Pelargoniumgrossularioides, Oleum cocoas, Laurus nobilis, Persea ameficana, Arachishypogaea, Linum usitatissimum, Linum humile, Linum austriacum, Linumbienne, Linum augustifolium, Linum catharticum, Linum flavum, Linumgrandiflorum, Adenolinum grandiflorum, Linum lewisii, Linum narbonense,Linum perenne, Linum perenne var. lewisii, Linum pratense, Linumtrigynum, Punica granatum, Gossypium hirsutum, Gossypium arboreum,Gossypium barbadense, Gossypium herbaceum, Gossypium thurberi, Musanana, Musa acuminata, Musa paradisiaca, Musa spp., Elaeis guineensis,Papaver orientate, Papaver rhoeas, Papaver dubium, Sesamum indicum,Piper aduncum, Piper amalago, Piper angustifolium, Piper auritum, Piperbetel, Piper cubeba, Piper longum, Piper nigrum, Piper retrofractum,Artanthe adunca, Artanthe elongata, Peperomia elongata, Piper elongatum,Steffensia elongata, Hordeum vulgare, Hordeum jubatum, Hordeum murinum,Hordeum secalinum, Hordeum distichon Hordeum aegiceras, Hordeumhexastichon., Hordeum hexastichum, Hordeum irregulare, Hordeum sativum,Hordeum secalinum, Avena sativa, Avena fatua, Avena byzantina, Avenafatua var. sativa, Avena hybrida, Sorghum bicolor, Sorghum halepense,Sorghum saccharatum, Sorghum vulgare, Andropogon drummondii, Holcusbicolor, Holcus sorghum, Sorghum aethiopicum, Sorghum arundinaceum,Sorghum caffrorum, Sorghum cernuum, Sorghum dochna, Sorghum drummondii,Sorghum durra, Sorghum guineense, Sorghum lanceolatum, Sorghum nervosum,Sorghum saccharatum, Sorghum subglabrescens, Sorghum verticilliflorum,Sorghum vulgare, Holcus halepensis, Sorghum mlliaceum millet, Panicummilitaceum, Zea mays, Triticum aestivum, Triticum durum, Triticumturgidum, Triticum hybernum, Triticum macha, Triticum sativum orTriticum vulgare, Cofea spp., Coffea arabica, Coffea canephora, Coffealiberica, Capsicum annuum, Capsicum annuum var. glabriusculum, Capsicumfrutescens, Capsicum annuum, Nicotiana tabacum, Solanum tuberosum,Solanum metongena, Lycopersicon esculentum, Lycopersicon lycopersicum,Lycopersicon pyriforme, Solanum integrifolium, Solanum lycopersicumTheobroma cacao or Camellia sinensis.

Anacardiaceae such as the genera Pistacia, Mangifera, Anacardium e.g.the species Pistacia vera [pistachios, Pistazie], Mangifer indica[Mango] or Anacardium occidentale [Cashew]; Asteraceae such as thegenera Calendula, Carthamus, Centaurea, Cichorium, Cynara, Helianthus,Lactuca, Locusta, Tagetes, Valeriana e.g. the species Calendulaofficinags [Marigold], Carthamus tinctorius [safflower], Centaureacyanus [cornflower], Cichorium intybus [blue daisy], Cynara scolymus[Artichoke], Helianthus annus [sunflower], Lactuca sativa, Lactucacrispa, Lactuca esculenta, Lactuca scariola L. ssp. sativa, Lactucascariola L. var. integrata, Lactuca scariola L. var. integrifolia,Lactuca sativa subsp. roman, Locusta communis, Vaterian locusta[lettuce], Tagetes lucida, Tagetes erecta or Tagetes tenuifolia[Marigold]; Apiaceae such as the genera Daucus e.g. the species Daucuscarota [carrot]; Betulaceae such as the genera Corylus e.g. the speciesCorylus aveilana or Corylus colurna [hazelnut]; Boraginaceae such as thegenera Borago e.g. the species Borago officinalis [borage]; Brassicaceaesuch as the genera Brassica, Melanosinapis, Sinapis, Arabadopsis e.g.the species Brassica napus, Brassica raga ssp. [canola, oilseed rape,turnip rape], Sinapis arvensis Brassica juncea, Brassica juncea var.juncea, Brassica juncea var. crispifolia, Brassica juncea var. foliosa,Brassica nigra, Brassica sinapioides, Melanosinapis communis [mustard],Brassica oteracea [fodder beet] or Arabidopsis thaliana; Bromeliaceaesuch as the genera Anana, Bromelia e.g. the species Anana comosus,Ananas ananas or Bromelia comosa [pineapple]; Caricaceae such as thegenera Carica e.g. the species Carica papaya [papaya]; Cannabaceae suchas the genera Cannabis e.g. the species Cannbis sative [hemp],Convolvulaceae such as the genera Ipomea, Convolvulus e.g. the speciesIpomoea batatus, Ipomoea pandurata, Convolvulus batatas, Convolvulustikaceus, Ipomoea fastigiata, Ipomoea tiliacea, Ipomoea triloba orConvolvulus panduratus [sweet potato, Man of the Earth, wild potato],Chenopodiaceae such as the genera Beta, i.e. the species Beta vulgaris,Beta vulgaris var. altissima, Beta vulgaris var. Vulgaris, Betamaritima, Beta vulgaris var. perennis, Beta vulgaris var conditiva orBeta vulgaris var. esculenta [sugar beet]; Cucurbitaceae such as thegenera Cucubita e.g. the species Cucurbita maxima, Cucurbita mixta,Cucurbita pepo or Cucurbita moschata [pumpkin, squash]; Elaeagnaceaesuch as the genera Elaeagnus e.g. the species Olea europaea [olive];Ericaceae such as the genera Kalmia e.g. the species Kalmia latifoka,Kalmia angustifolia, Kalmia microphylla, Kalmia polifoka, Kalmiaoccidentalis, Cistus chamaerhodendros or Kalmia lucida [American laurel,broad-leafed laurel, calico bush, spoon wood, sheep laurel, alpinelaurel, bog laurel, western bog-laurel, swamp-laurel]; Euphorbiaceaesuch as the genera Manihot, Janipha, Jatropha, Ricinus e.g. the speciesManihot ultissima, Janipha manihot, Jatropha manihot, Manihot aipil,Manihot dulcis, Manihot manihot, Manihot melanobasis, Manihot esculenta[manihot, arrowroot, tapioca, cassava] or Ricinus communis [castor bean,Castor Oil Bush, Castor Oil Plant, Palma Christi, Wonder Tree]; Fabaceaesuch as the genera Pisum, Albizia, Cathormion, Feuillea, Inga,Pithecolobium, Acacia, Mimosa, Medicajo, Glycine, Dolichos, Phaseolus,Soja e.g. the species Pisum sativum, Pisum arvense, Pisum humile [pea],Albizia bertenana, Albizia julibrissin, Albizia lebbeck, Acaciabertenana, Acacia littoralis, Albizia bertenana, Albizzia bertenana,Cathormion bertenana, Feuillea bertenana, Inga fragrans, Pithecellobiumbertenanum, Pithecellobium fragrans, Pithecolobium bertenanum,Pseudalbizzia bertenana, Acacia jukbrissin, Acacia nemu, Albizia nemu,Feuilleea julibrissin, Mimosa julibrissin, Mimosa speciosa, Sericanrdajulibrissin, Acacia lebbeck, Acacia macrophylla, Albizia lebbek,Feuilleea lebbeck, Mimosa lebbeck, Mimosa speciosa [bastard logwood,silk tree, East Indian Walnut], Medicago sativa, Medicago falcata,Medicago varia [alfalfa] Glycine max Dolichos soja, Glycine gracilis,Glycine hispida, Phaseolus max, Soja hispida or Soja max [soybean];Geraniaceae such as the genera Pelargonium, Cocos, Oleum e.g. thespecies Cocos nucifera, Pelargonium grossulariodes or Oleum cocois[coconut]; Gramineae such as the genera Saccharum e.g. the speciesSaccharum officinarum, Juglandaceae such as the genera Juglans, Walliae.g. the species Juglans regia, Juglans ailanthifoka, Juglanssieboldiana, Juglans cinerea, Walka cinerea, Juglans bixbyi, Juglanscalifornica, Juglans hindsii, Juglans intermedia, Juglans jamaicensis,Juglans major, Juglans microcarpa, Juglans nigra or Wallia nigra[walnut, black walnut, common walnut, persian walnut, white walnut,butternut, black walnut]; Lauraceae such as the genera Persea, Lauruse.g. the species laurel Laurus nobilis [bay, laurel, bay laurel, sweetbay], Persea americana Persea americana, Persea gratissima or Perseapersea [avocado]; Leguminosae such as the genera Arachis e.g. thespecies Arachis hypogaea [peanut]; Linaceae such as the genera Linum,Adenolinum e.g. the species Linum usitatissimum, Linum humile, Linumaustriacum, Linum bienne, Linum angustifolium, Linum catharticum, Linumflavum, Linum grandiflorum, Adenoknum grandiflorum, Linum lewisii, Linumnarbonense, Linum perenne, Linum perenne var. lewisii, Linum pratense orLinum trigynum [flax, linseed]; Lythrarieae such as the genera Punicae.g. the species Punica granatum [pomegranate]; Malvaceae such as thegenera Gossypium e.g. the species Gossypium hirsutum, Gossypiumarboreum, Gossypium barbadense, Gossypium herbaceum or Gossypiumthurberi [cotton]; Musaceae such as the genera Musa e.g. the speciesMusa nana, Musa acuminata, Musa paradisiaca, Musa spp. [banana];Onagraceae such as the genera Camissonia, Oenothera e.g. the speciesOenothera biennis or Camissonia brevipes [primrose, evening primrose];Palmae such as the genera Elacis e.g. the species Elaeiis guineensis[oil plam]; Papaveraceae such as the genera Papaver e.g. the speciesPapaver orientate, Papaver rhoeas, Papaver dubium [poppy, orientalpoppy, corn poppy, field poppy, shirley poppies, field poppy,long-headed poppy, long-pod poppy]; Pedaliaceae such as the generaSesamum e.g. the species Sesamum indicum [sesame]; Piperaceae such asthe genera Piper, Artanthe, Peperomia, Steffensia e.g. the species Piperaduncum, Piper amalago, Piper angustifolium, Piper auritum, Piper betelPiper cubeba, Piper longum, Piper nigrum, Piper retrofractum, Artantheadunca, Artanthe elongata, Peperomia elongata, Piper elongatum,Steffensia elongata. [Cayenne pepper, wild pepper]; Poaceae such as thegenera Hordeum, Secale, Avena, Sorghum, Andropogon, Holcus, Panicum,Oryza, Zea, Triticum e.g. the species Hordeum vulgare, Hordeum jubatum,Hordeum munnum, Hordeum secalinum, Hordeum distichon Hordeum aegiceras,Hordeum hexastichon., Hordeum hexastichum, Hordeum irregulare, Hordeumsativum, Hordeum secalinum [barley, pearl barley, foxtail barley, wallbarley, meadow barley], Secale cereale [rye], Avena sativa, Avena fatua,Avena byzantina, Avena fatua var. sativa, Avena hybrida [oat], Sorghumbicolor, Sorghum halepense, Sorghum saccharatum, Sorghum vulgare,Andropogon drummondii, Holcus bicolor, Holcus sorghum, Sorghumaethiopicum, Sorghum arundinaceum, Sorghum caffrorum, Sorghum cernuum,Sorghum dochna, Sorghum drummondii, Sorghum durra, Sorghum guineense,Sorghum lanceolatum, Sorghum nervosum, Sorghum saccharatum, Sorghumsubglabrescens, Sorghum verticilliflorum, Sorghum vulgare, Holcushalepensis, Sorghum miliaceum millet, Panicum militaceum [Sorghum,millet], Oryza sativa, Oryza latifolia [rice], Zea mays [corn, maize]Triticum aestivum, Triticum durum, Triticum turgidum, Triticum hybernum,Triticum macha, Triticum sativum or Triticum vulgare [wheat, breadwheat, common wheat], Proteaceae such as the genera Macadamia e.g. thespecies Macadamia intergrifolia [macadamia]; Rubiaceae such as thegenera Coffea e.g. the species Cofea spp., Coffea arabica, Coffeacanephora or Coffea liberica [coffee]; Scrophulariaceae such as thegenera Verbascum e.g. the species Verbascum blattana, Verbascum chaixii,Verbascum densiflorum, Verbascum lagurus, Verbascum longifolium,Verbascum lychnitis, Verbascum nigrum, Verbascum olympibum, Verbascumphlomoides, Verbascum phoenicum, Verbascum pulverulentum or Verbascumthapsus [mullein, white moth mullein, nettle-leaved mullein,dense-flowered mullein, silver mullein, long-leaved mullein, whitemullein, dark mullein, greek mullein, orange mullein, purple mullein,hoary mullein, great mullein]; Solanaceae such as the genera Capsicum,Nicotiana, Solanum, Lycopersicon e.g. the species Capsicum annuum,Capsicum annuum var. glabriusculum, Capsicum frutescens [pepper],Capsicum annuum [paprika], Nicotiana tabacum, Nicotiana alata, Nicotianaattenuata, Nicotiana glauca, Nicotiana langsdorffii, Nicotianaobtusifolia, Nicotiana quadrivalvis, Nicotiana repanda, Nicotianarustica, Nicotiana sylvestris [tobacco], Solanum tuberosum [potato],Solanum melongena [egg-plant] (Lycopersicon esculentum, Lycopersiconlycopersicum., Lycopersicon pyriforme, Solanum integrifolium or Solanumlycopersicum [tomato]; Sterculiaceae such as the genera Theobroma e.g.the species Theobroma cacao [cacao]; Theaceae such as the generaCamellia e.g. the species Camellia sinensis) [tea].

The introduction of the nucleic acids according to the invention, theexpression cassette or the vector into organisms, plants for example,can in principle be done by all of the methods known to those skilled inthe art. The introduction of the nucleic acid sequences gives rise torecombinant or transgenic organisms.

Unless otherwise specified, the terms “polynucleotides”, “nucleic acid”and “nucleic acid molecule” as used herein are interchangeably. Unlessotherwise specified, the terms “peptide”, “polypeptide” and “protein”are interchangeably in the present context. The term “sequence” mayrelate to polynucleotides, nucleic acids, nucleic acid molecules,peptides, polypeptides and proteins, depending on the context in whichthe term “sequence” is used. The terms “gene(s)”, “polynucleotide”,“nucleic acid sequence”, “nucleotide sequence”, or “nucleic acidmolecule(s)” as used herein refers to a polymeric form of nucleotides ofany length, either ribonucleotides or deoxyribonucleotides. The termsrefer only to the primary structure of the molecule.

Thus, the terms “gene(s)”, “polynucleotide”, “nucleic acid sequence”,“nucleotide sequence”, or “nucleic acid molecule(s)” as used hereininclude double- and single-stranded DNA and RNA. They also include knowntypes of modifications, for example, methylation, “caps”, substitutionsof one or more of the naturally occurring nucleotides with an analog.Preferably, the DNA or RNA sequence of the invention comprises a codingsequence encoding the herein defined polypeptide.

The genes of the invention, coding for an activity selected from thegroup consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-ketosterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T/prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease are also called “NUERP gene”.

A “coding sequence” is a nucleotide sequence, which is transcribed intomRNA and/or translated into a polypeptide when placed under the controlof appropriate regulatory sequences. The boundaries of the codingsequence are determined by a translation start codon at the 5′-terminusand a translation stop codon at the 3′-terminus. The triplets taa, tgaand tag represent the (usual) stop codons which are interchangeable. Acoding sequence can include, but is not limited to mRNA, cDNA,recombinant nucleotide sequences or genomic DNA, while introns may bepresent as well under certain circumstances.

The transfer of foreign genes into the genome of a plant is calledtransformation. In doing this the methods described for thetransformation and regeneration of plants from plant tissues or plantcells are utilized for transient or stable transformation. Suitablemethods are protoplast transformation by poly(ethylene glycol)-inducedDNA uptake, the “biolistic” method using the gene cannon—referred to asthe particle bombardment method, electroporation, the incubation of dryembryos in DNA solution, microinjection and gene transfer mediated byAgrobacterium. Said methods are described by way of example in Jenes B.et al., Techniques for Gene Transfer, in: Transgenic Plants, Vol. 1,Engineering and Utilization, eds. Kung S. D and Wu R., Academic Press(1993) 128-143 and in Potrykus, Annu. Rev. Plant Physiol. Plant Molec.Biol. 42, 205 (1991). The nucleic acids or the construct to be expressedis preferably cloned into a vector which is suitable for transformingAgrobacterium tumefaciens, for example pBin19 (Bevan et al., Nucl. AcidsRes. 12, 8711 (1984)). Agrobacteria transformed by such a vector canthen be used in known manner for the transformation of plants, inparticular of crop plants such as by way of example tobacco plants, forexample by bathing bruised leaves or chopped leaves in an agrobacterialsolution and then culturing them in suitable media. The transformationof plants by means of Agrobacterium tumefaciens is described, forexample, by Höfgen and Willmitzer in Nucl. Acid Res. 16, 9877 (1988) oris known inter alia from White F.F., Vectors for Gene Transfer in HigherPlants; in Transgenic Plants, Vol. 1, Engineering and Utilization, eds.Kung S.D. and Wu R., Academic Press, 1993, pp. 15-38.

Agrobacteria transformed by an expression vector according to theinvention may likewise be used in known manner for the transformation ofplants such as test plants like Arabidopsis or crop plants such ascereal crops, corn, oats, rye, barley, wheat, soybean, rice, cotton,sugar beet, canola, sunflower, flax, hemp, potatoes, tobacco, tomatoes,carrots, paprika, oilseed rape, tapioca, cassava, arrowroot, tagetes,alfalfa, lettuce and the various tree, nut and vine species, inparticular oil-containing crop plants such as soybean, peanut, castoroil plant, sunflower, corn, cotton, flax, oilseed rape, coconut, oilpalm, safflower (Carthamus tinctorius) or cocoa bean, or in particularcorn, wheat, soybean, rice, cotton and canola, e.g. by bathing bruisedleaves or chopped leaves in an agrobacterial solution and then culturingthem in suitable media.

The genetically modified plant cells may be regenerated by all of themethods known to those skilled in the art. Appropriate methods can befound in the publications referred to above by Kung S.D. and Wu R.,Potrykus or Höfgen and Willmitzer.

Accordingly, a further aspect of the invention relates to transgenicorganisms transformed by at least one nucleic acid sequence, expressioncassette or vector according to the invention as well as cells, cellcultures, tissue, parts—such as, for example, leaves, roots, etc. in thecase of plant organisms—or reproductive material derived from suchorganisms. The terms “host organism”, “host cell”, “recombinant (host)organism” and “transgenic (host) cell” are used here interchangeably. Ofcourse these terms relate not only to the particular host organism orthe particular target cell but also to the descendants or potentialdescendants of these organisms or cells. Since, due to mutation orenvironmental effects certain modifications may arise in successivegenerations, these descendants need not necessarily be identical withthe parental cell but nevertheless are still encompassed by the term asused here.

For the purposes of the invention “transgenic” or “recombinant” meanswith regard for example to a nucleic acid sequence, an expressioncassette (=gene construct, nucleic acid construct) or a vectorcontaining the nucleic acid sequence according to the invention or anorganism transformed by the nucleic acid sequences, expression cassetteor vector according to the invention all those constructions produced bygenetic engineering methods in which either

-   (a) the nucleic acid sequence depicted in table I, application no.    1, column 5 or 7 or its derivatives or parts thereof; or-   (b) a genetic control sequence functionally linked to the nucleic    acid sequence described under (a), for example a 3′- and/or    5′-genetic control sequence such as a promoter or terminator, or-   (c) (a) and (b);    are not found in their natural, genetic environment or have been    modified by genetic engineering methods, wherein the modification    may by way of example be a substitution, addition, deletion,    inversion or insertion of one or more nucleotide residues. Natural    genetic environment means the natural genomic or chromosomal locus    in the organism of origin or inside the host organism or presence in    a genomic library. In the case of a genomic library the natural    genetic environment of the nucleic acid sequence is preferably    retained at least in part. The environment borders the nucleic acid    sequence at least on one side and has a sequence length of at least    50 bp, preferably at least 500 bp, particularly preferably at least    1,000 bp, most particularly preferably at least 5,000 bp. A    naturally occurring expression cassette—for example the naturally    occurring combination of the natural promoter of the nucleic acid    sequence according to the invention with the corresponding    gene—turns into a transgenic expression cassette when the latter is    modified by unnatural, synthetic (“artificial”) methods such as by    way of example a mutagenation. Appropriate methods are described by    way of example in U.S. Pat. No. 5,565,350 or WO 00/15815.

Suitable organisms or host organisms for the nucleic acid, expressioncassette or vector according to the invention are advantageously inprinciple all organisms, which are suitable for the expression ofrecombinant genes as described above. Further examples which may bementioned are plants such as Arabidopsis, Asteraceae such as Calendulaor crop plants such as soybean, peanut, castor oil plant, sunflower,flax, corn, cotton, flax, oilseed rape, coconut, oil palm, safflower(Carthamus tinctorius) or cocoa bean.

In one embodiment of the invention host plants for the nucleic acid,expression cassette or vector according to the invention are selectedfrom the group comprising corn, soy, oil seed rape (including canola andwinter oil seed rape), cotton, wheat and rice.

A further object of the invention relates to the use of a nucleic acidconstruct, e.g. an expression cassette, containing DNA sequencesencoding polypeptides shown in table II or DNA sequences hybridizingtherewith for the transformation of plant cells, tissues or parts ofplants.

In doing so, depending on the choice of promoter, the sequences shown intable I can be expressed specifically in the leaves, in the seeds, thenodules, in roots, in the stem or other parts of the plant. Thosetransgenic plants overproducing sequences as depicted in table I, thereproductive material thereof, together with the plant cells, tissues orparts thereof are a further object of the present invention.

The expression cassette or the nucleic acid sequences or constructaccording to the invention containing sequences according to table Ican, moreover, also be employed for the transformation of the organismsidentified by way of example above such as bacteria, yeasts, filamentousfungi and plants.

Within the framework of the present invention, increased yield,especially enhanced NUE and/or biomass production, means, for example,the artificially acquired trait of increased yield, especially ofenhanced NUE and/or biomass production, due to functional overexpression of polypeptide sequences of table II encoded by thecorresponding nucleic acid molecules as depicted in table I, column 5 or7 and/or homologs in the organisms according to the invention,advantageously in the transgenic plants according to the invention, bycomparison with the nongenetically modified initial plants at least forthe duration of at least one plant generation.

A constitutive expression of the polypeptide sequences of table II,application no. 1, encoded by the corresponding nucleic acid molecule asdepicted in table I, application no. 1, column 5 or 7 and/or homologsis, moreover, advantageous. On the other hand, however, an inducibleexpression may also appear desirable. Expression of the polypeptidesequences of the invention can be either direct to the cytoplasm or theorganelles, preferably the plastids of the host cells, preferably theplant cells.

The efficiency of the expression of the sequences of the of table II,application no. 1, encoded by the corresponding nucleic acid molecule asdepicted in table I, application no. 1, column 5 or 7 and/or homologscan be determined, for example, in vitro by shoot meristem propagation.In addition, an expression of the sequences of table II, application no.1, encoded by the corresponding nucleic acid molecule as depicted intable I, application no. 1, column 5 or 7 and/or homologs modified innature and level and its effect effect on yield, particularly toleranceto abiotic environmental stress and/or nutrient use efficiency, but alsoon the metabolic pathways performance can be tested on test plants ingreenhouse trials.

An additional object of the invention comprises transgenic organismssuch as transgenic plants transformed by an expression cassettecontaining sequences of as depicted in table I, application no. 1,column 5 or 7 according to the invention or DNA sequences hybridizingtherewith, as well as transgenic cells, tissue, parts and reproductionmaterial of such plants. Particular preference is given in this case totransgenic crop plants such as by way of example barley, wheat, rye,oats, corn, soybean, rice, cotton, sugar beet, oilseed rape and canola,sunflower, flax, hemp, thistle, potatoes, tobacco, tomatoes, tapioca,cassava, arrowroot, alfalfa, lettuce and the various tree, nut and vinespecies.

In one embodiment of the invention transgenic plants transformed by anexpression cassette containing sequences of as depicted in table I,application no. 1, column 5 or 7 according to the invention or DNAsequences hybridizing therewith are selected from the group comprisingcorn, soy, oil seed rape (including canola and winter oil seed rape),cotton, wheat and rice.

For the purposes of the invention plants are mono- and dicotyledonousplants, mosses or algae, especially plants, preferably monocotyledonousplants, or preferably dicotyledonous plants.

A further refinement according to the invention are transgenic plants asdescribed above which contain a nucleic acid sequence or constructaccording to the invention or a expression cassette according to theinvention.

However, transgenic also means that the nucleic acids according to theinvention are located at their natural position in the genome of anorganism, but that the sequence has been modified in comparison with thenatural sequence and/or that the regulatory sequences of the naturalsequences have been modified. Preferably, transgenic/recombinant is tobe understood as meaning the transcription of the nucleic acids of theinvention and shown in table I, occurs at a non-natural position in thegenome, that is to say the expression of the nucleic acids is homologousor, preferably, heterologous. This expression can be transiently or of asequence integrated stably into the genome.

The term “transgenic plants” used in accordance with the invention alsorefers to the progeny of a transgenic plant, for example the T1, T2, T3and subsequent plant generations or the BC1, BC2, BC3 and subsequentplant generations. Thus, the transgenic plants according to theinvention can be raised and selfed or crossed with other individuals inorder to obtain further transgenic plants according to the invention.Transgenic plants may also be obtained by propagating transgenic plantcells vegetatively. The present invention also relates to transgenicplant material, which can be derived from a transgenic plant populationaccording to the invention. Such material includes plant cells andcertain tissues, organs and parts of plants in all their manifestations,such as seeds, leaves, anthers, fibers, tubers, roots, root hairs,stems, embryo, calli, cotelydons, petioles, harvested material, planttissue, reproductive tissue and cell cultures, which are derived fromthe actual transgenic plant and/or can be used for bringing about thetransgenic plant.

Any transformed plant obtained according to the invention can be used ina conventional breeding scheme or in vitro plant propagation to producemore transformed plants with the same characteristics and/or can be usedto introduce the same characteristic in other varieties of the same orrelated species. Such plants are also part of the invention. Seedsobtained from the transformed plants genetically also contain the samecharacteristic and are part of the invention. As mentioned before, thepresent invention is in principle applicable to any plant and crop thatcan be transformed with any of the transformation method known to thoseskilled in the art.

Advantageous inducible plant promoters are by way of example the PRP1promoter (Ward et al., Plant. Mol. Biol. 22361 (1993)), a promoterinducible by benzenesulfonamide (EP 388 186), a promoter inducible bytetracycline (Gatz et al., Plant J. 2, 397 (1992)), a promoter inducibleby salicylic acid (WO 95/19443), a promoter inducible by abscisic acid(EP 335 528) and a promoter inducible by ethanol or cyclohexanone (WO93/21334). Other examples of plant promoters which can advantageously beused are the promoter of cytosolic FBPase from potato, the ST-LSIpromoter from potato (Stockhaus et al., EMBO J. 8, 2445 (1989)), thepromoter of phosphoribosyl pyrophosphate amidotransferase from Glycinemax (see also gene bank accession number U87999) or a nodiene-specificpromoter as described in EP 249 676. Particular advantageous are thosepromoters which ensure expression upon conditions of limited nutrientavailability, e.g. the onset of limited nitrogen sources in case thenitrogen of the soil or nutrient is exhausted, and/or expression upon atthe onset of chilling and/or freezing temperatures and/or waterdeficiency, as defined hereinabove. Such promotors are known to theperson skilled in the art or can be isolated from genes which areinduced under the conditions mentioned above.

In one embodiment seed-specific promoters may be used formonocotyledonous or dicotyledonous plants.

In principle all natural promoters with their regulation sequences canbe used like those named above for the expression cassette according tothe invention and the method according to the invention. Over and abovethis, synthetic promoters may also advantageously be used.

In the preparation of an expression cassette various DNA fragments canbe manipulated in order to obtain a nucleotide sequence, which usefullyreads in the correct direction and is equipped with a correct readingframe. To connect the DNA fragments (=nucleic acids according to theinvention) to one another adaptors or linkers may be attached to thefragments.

The promoter and the terminator regions can usefully be provided in thetranscription direction with a linker or polylinker containing one ormore restriction points for the insertion of this sequence. Generally,the linker has 1 to 10, mostly 1 to 8, preferably 2 to 6, restrictionpoints. In general the size of the linker inside the regulatory regionis less than 100 bp, frequently less than 60 bp, but at least 5 bp. Thepromoter may be both native or homologous as well as foreign orheterologous to the host organism, for example to the host plant. In the5′-3′ transcription direction the expression cassette contains thepromoter, a DNA sequence which shown in table I and a region fortranscription termination. Different termination regions can beexchanged for one another in any desired fashion.

As also used herein, the terms “nucleic acid” and “nucleic acidmolecule” are intended to include DNA molecules (e.g. cDNA or genomicDNA) and RNA molecules (e.g. mRNA) and analogs of the DNA or RNAgenerated using nucleotide analogs. This term also encompassesuntranslated sequence located at both the 3′ and 5′ ends of the codingregion of the gene—at least about 1000 nucleotides of sequence upstreamfrom the 5′ end of the coding region and at least about 200 nucleotidesof sequence downstream from the 3′ end of the coding region of the gene.The nucleic acid molecule can be single-stranded or double-stranded, butpreferably is double-stranded DNA.

An “isolated” nucleic acid molecule is one that is substantiallyseparated from other nucleic acid molecules, which are present in thenatural source of the nucleic acid. That means other nucleic acidmolecules are present in an amount less than 5% based on weight of theamount of the desired nucleic acid, preferably less than 2% by weight,more preferably less than 1% by weight, most preferably less than 0.5%by weight. Preferably, an “isolated” nucleic acid is free of some of thesequences that naturally flank the nucleic acid (i.e., sequences locatedat the 5′ and 3′ ends of the nucleic acid) in the genomic DNA of theorganism from which the nucleic acid is derived. For example, in variousembodiments, the isolated NUE related protein (NUERP) encoding nucleicacid molecule can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb,0.5 kb or 0.1 kb of nucleotide sequences which naturally flank thenucleic acid molecule in genomic DNA of the cell from which the nucleicacid is derived. Moreover, an “isolated” nucleic acid molecule, such asa cDNA molecule, can be free from some of the other cellular materialwith which it is naturally associated, or culture medium when producedby recombinant techniques, or chemical precursors or other chemicalswhen chemically synthesized.

A nucleic acid molecule of the present invention, e.g., a nucleic acidmolecule encoding an NUERP or a portion thereof which confers enhancedtolerance to abiotic environmental stress and/or enhanced nutrient useefficiency and/or increased yield, especially enhanced NUE and/orincreased biomass production, in plants, can be isolated using standardmolecular biological techniques and the sequence information providedherein. For example, an Arabidopsis thaliana NUERP encoding cDNA can beisolated from a A. thaliana c-DNA library or a Synechocystis sp.,Brassica napus, Glycine max, Zea mays or Oryza sativa NUERP encodingcDNA can be isolated from a Synechocystis sp., Brassica napus, Glycinemax, Zea mays or Oryza sativa c-DNA library respectively using all orportion of one of the sequences shown in table I. Moreover, a nucleicacid molecule encompassing all or a portion of one of the sequences oftable I can be isolated by the polymerase chain reaction usingoligonucleotide primers designed based upon this sequence. For example,mRNA can be isolated from plant cells (e.g., by theguanidinium-thiocyanate extraction procedure of Chirgwin et al.,Biochemistry 18, 5294 (1979)) and cDNA can be prepared using reversetranscriptase (e.g., Moloney MLV reverse transcriptase, available fromGibco/BRL, Bethesda, Md.; or AMV reverse transcriptase, available fromSeikagaku America, Inc., St. Petersburg, Fla.). Syntheticoligonucleotide primers for polymerase chain reaction amplification canbe designed based upon one of the nucleotide sequences shown in table I.A nucleic acid molecule of the invention can be amplified using cDNA or,alternatively, genomic DNA, as a template and appropriateoligonucleotide primers according to standard PCR amplificationtechniques. The nucleic acid molecule so amplified can be cloned into anappropriate vector and characterized by DNA sequence analysis.Furthermore, oligonucleotides corresponding to a NUERP encodingnucleotide sequence can be prepared by standard synthetic techniques,e.g., using an automated DNA synthesizer.

In a preferred embodiment, an isolated nucleic acid molecule of theinvention comprises one of the nucleotide sequences shown in table Iencoding the NUERP (i.e., the “coding region”), as well as 5′untranslated sequences and 3′ untranslated sequences.

Moreover, the nucleic acid molecule of the invention can comprise only aportion of the coding region of one of the sequences of the nucleic acidof table I, for example, a fragment which can be used as a probe orprimer or a fragment encoding a biologically active portion of a NUERP.

Portions of proteins encoded by the NUERP encoding nucleic acidmolecules of the invention are preferably biologically active portionsdescribed herein. As used herein, the term “biologically active portionof” a NUERP is intended to include a portion, e.g. a domain/motif, ofNUE related protein (NUERP), which is sufficient to confer enhancedyield, particularly due to one or more improved yield related traits asdefined above, especially which participates in an enhanced NUEefficiency and/or increased biomass production, in a plant. To determinewhether a NUERP, or a biologically active portion thereof, results in anenhanced yield, particularly due to one or more improved yield relatedtraits as defined above, especially an enhanced NUE efficiency and/orincreased biomass production, in a plant, an analysis of a plantcomprising the NUERP may be performed. Such analysis methods are wellknown to those skilled in the art, as detailed in the Examples. Morespecifically, nucleic acid fragments encoding biologically activeportions of a NUERP can be prepared by isolating a portion of one of thesequences of the nucleic acid of table I expressing the encoded portionof the NUERP or peptide (e.g., by recombinant expression in vitro) andassessing the activity of the encoded portion of the NUERP or peptide.

Biologically active portions of a NUERP are encompassed by the presentinvention and include peptides comprising amino acid sequences derivedfrom the amino acid sequence of a NUERP encoding gene, or the amino acidsequence of a protein homologous to a NUERP, which include fewer aminoacids than a full length NUERP or the full length protein which ishomologous to a NUERP, and exhibits at least some enzymatic orbiological activity of a NUERP. Typically, biologically active portions(e.g., peptides which are, for example, 5, 10, 15, 20, 30, 35, 36, 37,38, 39, 40, 50, 100 or more amino acids in length) comprise a domain ormotif with at least one activity of a NUERP. Moreover, otherbiologically active portions in which other regions of the protein aredeleted, can be prepared by recombinant techniques and evaluated for oneor more of the activities described herein. Preferably, the biologicallyactive portions of a NUERP include one or more selected domains/motifsor portions thereof having biological activity.

The term “biological active portion” or “biological activity” means apolypeptide as depicted in table II, column 3 or a portion of saidpolypeptide which still has at least 10% or 20%, preferably 30%, 40%,50% or 60%, especially preferably 70%, 75%, 80%, 90% or 95% of theenzymatic or biological activity of the natural or starting enzyme orprotein.

In the process according to the invention nucleic acid sequences can beused, which, if appropriate, contain synthetic, non-natural or modifiednucleotide bases, which can be incorporated into DNA or RNA. Saidsynthetic, non-natural or modified bases can for example increase thestability of the nucleic acid molecule outside or inside a cell. Thenucleic acid molecules of the invention can contain the samemodifications as aforementioned.

As used in the present context the term “nucleic acid molecule” may alsoencompass the untranslated sequence located at the 3′ and at the 5′ endof the coding gene region, for example at least 500, preferably 200,especially preferably 100, nucleotides of the sequence upstream of the5′ end of the coding region and at least 100, preferably 50, especiallypreferably 20, nucleotides of the sequence downstream of the 3′ end ofthe coding gene region. It is often advantageous only to choose thecoding region for cloning and expression purposes.

Preferably, the nucleic acid molecule used in the process according tothe invention or the nucleic acid molecule of the invention is anisolated nucleic acid molecule.

An “isolated” polynucleotide or nucleic acid molecule is separated fromother polynucleotides or nucleic acid molecules, which are present inthe natural source of the nucleic acid molecule. An isolated nucleicacid molecule may be a chromosomal fragment of several kb, orpreferably, a molecule only comprising the coding region of the gene.Accordingly, an isolated nucleic acid molecule of the invention maycomprise chromosomal regions, which are adjacent 5′ and 3′ or furtheradjacent chromosomal regions, but preferably comprises no such sequenceswhich naturally flank the nucleic acid molecule sequence in the genomicor chromosomal context in the organism from which the nucleic acidmolecule originates (for example sequences which are adjacent to theregions encoding the 5′- and 3′-UTRs of the nucleic acid molecule).

In various embodiments, the isolated nucleic acid molecule used in theprocess according to the invention may, for example comprise less thanapproximately 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb or 0.1 kb nucleotidesequences which naturally flank the nucleic acid molecule in the genomicDNA of the cell from which the nucleic acid molecule originates.

The nucleic acid molecules used in the process, for example thepolynucleotide of the invention or of a part thereof can be isolatedusing molecularbiological standard techniques and the sequenceinformation provided herein. Also, for example a homologous sequence orhomologous, conserved sequence regions at the DNA or amino acid levelcan be identified with the aid of comparison algorithms. The former canbe used as hybridization probes under standard hybridization techniques(for example those described in Sambrook et al., Molecular Cloning: ALaboratory Manual. 2nd Ed., Cold Spring Harbor Laboratory, Cold SpringHarbor Laboratory Press, Cold Spring Harbor, N.Y., 1989) for isolatingfurther nucleic acid sequences useful in this process.

A nucleic acid molecule encompassing a complete sequence of the nucleicacid molecules used in the process, for example the polynucleotide ofthe invention, or a part thereof may additionally be isolated bypolymerase chain reaction, oligonucleotide primers based on thissequence or on parts thereof being used. For example, a nucleic acidmolecule comprising the complete sequence or part thereof can beisolated by polymerase chain reaction using oligonucleotide primerswhich have been generated on the basis of this very sequence. Forexample, mRNA can be isolated from cells (for example by means of theguanidinium thiocyanate extraction method of Chirgwin et al.,Biochemistry 18, 5294 (1979)) and cDNA can be generated by means ofreverse transcriptase (for example Moloney MLV reverse transcriptase,available from Gibco/BRL, Bethesda, Md., or AMV reverse transcriptase,obtainable from Seikagaku America, Inc., St. Petersburg, Fla.).

Synthetic oligonucleotide primers for the amplification, e.g. as shownin table III, column 7, by means of polymerase chain reaction can begenerated on the basis of a sequence shown herein, for example thesequence shown in table I, application no. 1, columns 5 and 7 or thesequences derived from table II, application no. 1, columns 5 and 7.

Moreover, it is possible to identify conserved protein by carrying outprotein sequence alignments with the polypeptide encoded by the nucleicacid molecules of the present invention, in particular with thesequences encoded by the nucleic acid molecule shown in column 5 or 7 oftable I, application no. 1, from which conserved regions, and in turn,degenerate primers can be derived.

Conserved regions are those, which show a very little variation in theamino acid in one particular position of several homologs from differentorigin. The consenus sequence and polypeptide motifs shown in column 7of table IV, application no. 1, are derived from said alignments.Moreover, it is possible to identify conserved regions from variousorganisms by carrying out protein sequence alignments with thepolypeptide encoded by the nucleic acid of the present invention, inparticular with the sequences encoded by the polypeptide molecule shownin column 5 or 7 of table II, from which conserved regions, and in turn,degenerate primers can be derived.

In one advantageous embodiment, in the method of the present inventionthe activity of a polypeptide is increased comprising or consisting of aconsensus sequence or a polypeptide motif shown in table IV, applicationno. 1, column 7 and in one another embodiment, the present inventionrelates to a polypeptide comprising or consisting of a consensussequence or a polypeptide motif shown in table IV, application no. 1,column 7 whereby less than 20, preferably less than 15 or 10, preferablyless than 9, 8, 7, or 6, more preferred less than 5 or 4, even morepreferred less then 3, even more preferred less then 2, even morepreferred 0 of the amino acids positions indicated can be replaced byany amino acid. In one embodiment not more than 15%, preferably 10%,even more preferred 5%, 4%, 3%, or 2%, most preferred 1% or 0% of theamino acid position indicated by a letter are/is replaced another aminoacid. In one embodiment less than 20, preferably less than 15 or 10,preferably less than 9, 8, 7, or 6, more preferred less than 5 or 4,even more preferred less than 3, even more preferred less than 2, evenmore preferred 0 amino acids are inserted into a consensus sequence orprotein motif.

The consensus sequence was derived from a multiple alignment of thesequences as listed in table II. The letters represent the one letteramino acid code and indicate that the amino acids are conserved in atleast 80% of the aligned proteins. The letter X stands for amino acids,which are not conserved in at least 80% sequences. The consensussequence starts with the first conserved amino acid in the alignment,and ends with the last conserved amino acid in the alignment of theinvestigated sequences. The number of given X indicates the distancesbetween conserved amino acid residues, e.g. Y-x(21,23)-F means thatconserved tyrosine and phenylalanine residues are separated from eachother by minimum 21 and maximum 23 amino acid residues in allinvestigated sequences.

Conserved domains were identified from all sequences and are describedusing a subset of the standard Prosite notation, e.g. the patternY-x(21,23)-[FW] means that a conserved tyrosine is separated by minimum21 and maximum 23 amino acid residues from either a phenylalanine ortryptophane. Patterns had to match at least 80% of the investigatedproteins.

Conserved patterns were identified with the software tool MEME version3.5.1 or manually. MEME was developed by Timothy L. Bailey and CharlesElkan, Dept. of Computer Science and Engeneering, University ofCalifornia, San Diego, USA and is described by Timothy L. Bailey andCharles Elkan (Fitting a mixture model by expectation maximization todiscover motifs in biopolymers, Proceedings of the Second InternationalConference on Intelligent Systems for Molecular Biology, pp. 28-36, AAAIPress, Menlo Park, Calif., 1994). The source code for the stand-aloneprogram is public available from the San Diego Supercomputer center(http://meme.sdsc.edu).

For identifying common motifs in all sequences with the software toolMEME, the following settings were used: -maxsize 500000, -nmotifs 15,-evt 0.001, -maxw 60, -distance 1e-3, -minsites number of sequences usedfor the analysis. Input sequences for MEME were non-aligned sequences inFasta format. Other parameters were used in the default settings in thissoftware version.

Prosite patterns for conserved domains were generated with the softwaretool Pratt version 2.1 or manually. Pratt was developed by IngeJonassen, Dept. of Informatics, University of Bergen, Norway and isdescribed by Jonassen et al. (I. Jonassen, J.F.Collins and D.G.Higgins,Finding flexible patterns in unaligned protein sequences, ProteinScience 4 (1995), pp. 1587-1595; I.Jonassen, Efficient discovery ofconserved patterns using a pattern graph, Submitted to CABIOS Febr.1997]. The source code (ANSI C) for the stand-alone program is publicavailable, e.g. at established Bioinformatic centers like EBI (EuropeanBioinformatics Institute).

For generating patterns with the software tool Pratt, following settingswere used: PL (max Pattern Length): 100, PN (max Nr of Pattern Symbols):100, PX (max Nr of consecutive x's): 30, FN (max Nr of flexiblespacers): 5, FL (max Flexibility): 30, FP (max Flex.Product): 10, ON(max number patterns): 50. Input sequences for Pratt were distinctregions of the protein sequences exhibiting high similarity asidentified from software tool MEME. The minimum number of sequences,which have to match the generated patterns (CM, min Nr of Seqs to Match)was set to at least 80% of the provided sequences. Parameters notmentioned here were used in their default settings.

The Prosite patterns of the conserved domains can be used to search forprotein sequences matching this pattern. Various establishedBioinformatic centers provide public Internet portals for using thosepatterns in database searches (e.g. PIR (Protein Information Resource,located at Georgetown University Medical Center) or ExPASy (ExpertProtein Analysis System)). Alternatively, stand-alone software isavailable, like the program Fuzzpro, which is part of the EMBOSSsoftware package. For example, the program Fuzzpro not only allowssearching for an exact pattern-protein match but also allows settingvarious ambiguities in the performed search.

The alignment was performed with the software ClustalW (version 1.83)and is described by Thompson et al. (Nucleic Acids Research 22, 4673(1994)). The source code for the stand-alone program is public availablefrom the European Molecular Biology Laboratory; Heidelberg, Germany. Theanalysis was performed using the default parameters of ClustalW v1.83(gap open penalty: 10.0; gap extension penalty: 0.2; protein matrix:Gonnet; protein/DNA endgap: -1; protein/DNA gapdist: 4).

Degenerated primers can then be utilized by PCR for the amplification offragments of novel proteins having above-mentioned activity, e.g.conferring conferring the increase in yield, particularly enhancedtolerance to abiotic environmental stress and/or enhanced nutrient useefficiency, especially the enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, plant or part thereof after increasing the expression oractivity or having the activity of a protein as shown in table II,application no. 1, column 3 or further functional homologs of thepolypeptide of the invention from other organisms.

These fragments can then be utilized as hybridization probe forisolating the complete gene sequence. As an alternative, the missing 5′and 3′ sequences can be isolated by means of RACE-PCR. A nucleic acidmolecule according to the invention can be amplified using cDNA or, asan alternative, genomic DNA as template and suitable oligonucleotideprimers, following standard PCR amplification techniques. The nucleicacid molecule amplified thus can be cloned into a suitable vector andcharacterized by means of DNA sequence analysis. Oligonucleotides, whichcorrespond to one of the nucleic acid molecules used in the process, canbe generated by standard synthesis methods, for example using anautomatic DNA synthesizer.

Nucleic acid molecules which are advantageously for the processaccording to the invention can be isolated based on their homology tothe nucleic acid molecules disclosed herein using the sequences or partthereof as hybridization probe and following standard hybridizationtechniques under stringent hybridization conditions. In this context, itis possible to use, for example, isolated nucleic acid molecules of atleast 15, 20, 25, 30, 35, 40, 50, 60 or more nucleotides, preferably ofat least 15, or 25 nucleotides in length which hybridize under stringentconditions with the above-described nucleic acid molecules, inparticular with those which encompass a nucleotide sequence of thenucleic acid molecule used in the process of the invention or encoding aprotein used in the invention or of the nucleic acid molecule of theinvention. Nucleic acid molecules with 30, 50, 100, 250 or morenucleotides may also be used.

The term “homology” means that the respective nucleic acid molecules orencoded proteins are functionally and/or structurally equivalent. Thenucleic acid molecules that are homologous to the nucleic acid moleculesdescribed above and that are derivatives of said nucleic acid moleculesare, for example, variations of said nucleic acid molecules whichrepresent modifications having the same biological function, inparticular encoding proteins with the same or substantially the samebiological function. They may be naturally occurring variations, such assequences from other plant varieties or species, or mutations. Thesemutations may occur naturally or may be obtained by mutagenesistechniques. The allelic variations may be naturally occurring allelicvariants as well as synthetically produced or genetically engineeredvariants. Structurally equivalents can, for example, be identified bytesting the binding of said polypeptide to antibodies or computer basedpredictions. Structurally equivalents have the similar immunologicalcharacteristic, e.g. comprise similar epitopes.

By “hybridizing” it is meant that such nucleic acid molecules hybridizeunder conventional hybridization conditions, preferably under stringentconditions such as described by, e.g., Sambrook (Molecular Cloning; ALaboratory Manual, 2^(nd) Edition, Cold Spring Harbor Laboratory Press,Cold Spring Harbor, N.Y. (1989)) or in Current Protocols in MolecularBiology, John Wiley & Sons, N.Y. (1989), 6.3.1-6.3.6.

According to the invention, DNA as well as RNA molecules of the nucleicacid of the invention can be used as probes. Further, as template forthe identification of functional homologues Northern blot assays as wellas Southern blot assays can be performed. The Northern blot assayadvantageously provides further information about the expressed geneproduct: e.g. expression pattern, occurrence of processing steps, likesplicing and capping, etc. The Southern blot assay provides additionalinformation about the chromosomal localization and organization of thegene encoding the nucleic acid molecule of the invention.

A preferred, nonlimiting example of stringent hybridization conditionsare hybridizations in 6× sodium chloride/sodium citrate (═SSC) atapproximately 45° C., followed by one or more wash steps in 0.2×SSC,0.1% SDS at 50 to 65° C., for example at 50° C., 55° C. or 60° C. Theskilled worker knows that these hybridization conditions differ as afunction of the type of the nucleic acid and, for example when organicsolvents are present, with regard to the temperature and concentrationof the buffer. The temperature under “standard hybridization conditions”differs for example as a function of the type of the nucleic acidbetween 42° C. and 58° C., preferably between 45° C. and 50° C. in anaqueous buffer with a concentration of 0.1×, 0.5×, 1×, 2×, 3×, 4× or5×SSC (pH 7.2). If organic solvent(s) is/are present in theabovementioned buffer, for example 50% formamide, the temperature understandard conditions is approximately 40° C., 42° C. or 45° C. Thehybridization conditions for DNA:DNA hybrids are preferably for example0.1×SSC and 20° C., 25° C., 30° C., 35° C., 40° C. or 45° C., preferablybetween 30° C. and 45° C. The hybridization conditions for DNA:RNAhybrids are preferably for example 0.1×SSC and 30° C., 35° C., 40° C.,45° C., 50° C. or 55° C., preferably between 45° C. and 55° C. Theabovementioned hybridization temperatures are determined for example fora nucleic acid approximately 100 by (=base pairs) in length and a G+Ccontent of 50% in the absence of formamide. The skilled worker knows todetermine the hybridization conditions required with the aid oftextbooks, for example the ones mentioned above, or from the followingtextbooks: Sambrook et al., “Molecular Cloning”, Cold Spring HarborLaboratory, 1989; Hames and Higgins (Ed.) 1985, “Nucleic AcidsHybridization: A Practical Approach”, IRL Press at Oxford UniversityPress, Oxford; Brown (Ed.) 1991, “Essential Molecular Biology: APractical Approach”, IRL Press at Oxford University Press, Oxford.

A further example of one such stringent hybridization condition ishybridization at 4×SSC at 65° C., followed by a washing in 0.1×SSC at65° C. for one hour. Alternatively, an exemplary stringent hybridizationcondition is in 50% form amide, 4×SSC at 42° C. Further, the conditionsduring the wash step can be selected from the range of conditionsdelimited by low-stringency conditions (approximately 2×SSC at 50° C.)and high-stringency conditions (approximately 0.2×SSC at 50° C.,preferably at 65° C.) (20×SSC: 0.3 M sodium citrate, 3 M NaCl, pH 7.0).In addition, the temperature during the wash step can be raised fromlow-stringency conditions at room temperature, approximately 22° C., tohigher-stringency conditions at approximately 65° C. Both of theparameters salt concentration and temperature can be variedsimultaneously, or else one of the two parameters can be kept constantwhile only the other is varied. Denaturants, for example formamide orSDS, may also be employed during the hybridization. In the presence of50% formamide, hybridization is preferably effected at 42° C. Relevantfactors like 1) length of treatment, 2) salt conditions, 3) detergentconditions, 4) competitor DNAs, 5) temperature and 6) probe selectioncan be combined case by case so that not all possibilities can bementioned herein.

Thus, in a preferred embodiment, Northern blots are prehybridized withRothi-Hybri-Quick buffer (Roth, Karlsruhe) at 68° C. for 2 h.Hybridization with radioactive labelled probe is done overnight at 68°C. Subsequent washing steps are performed at 68° C. with 1×SSC.

For Southern blot assays the membrane is prehybridized withRothi-Hybri-Quick buffer (Roth, Karlsruhe) at 68° C. for 2 h. Thehybridization with radioactive labelled probe is conducted over night at68° C. Subsequently the hybridization buffer is discarded and the filtershortly washed using 2×SSC; 0,1% SDS. After discarding the washingbuffer new 2×SSC; 0,1% SDS buffer is added and incubated at 68° C. for15 minutes. This washing step is performed twice followed by anadditional washing step using 1×SSC; 0,1% SDS at 68° C. for 10 min.

Some examples of conditions for DNA hybridization (Southern blot assays)and wash step are shown herein below:

(1) Hybridization conditions can be selected, for example, from thefollowing conditions:

-   -   (a) 4×SSC at 65° C.,    -   (b) 6×SSC at 45° C.,    -   (c) 6×SSC, 100 mg/ml denatured fragmented fish sperm DNA at 68°        C.,    -   (d) 6×SSC, 0.5% SDS, 100 mg/ml denatured salmon sperm DNA at 68°        C.,    -   (e) 6×SSC, 0.5% SDS, 100 mg/ml denatured fragmented salmon sperm        DNA, 50% formamide at 42° C.,    -   (f) 50% formamide, 4×SSC at 42° C.,    -   (g) 50% (v/v) formamide, 0.1% bovine serum albumin, 0.1% Ficoll,        0.1% polyvinylpyrrolidone, 50 mM sodium phosphate buffer pH 6.5,        750 mM NaCl, 75 mM sodium citrate at 42° C.,    -   (h) 2× or 4×SSC at 50° C. (low-stringency condition), or    -   (i) 30 to 40% formamide, 2× or 4×SSC at 42° C. (low-stringency        condition).        (2) Wash steps can be selected, for example, from the following        conditions:    -   (a) 0.015 M NaCl/0.0015 M sodium citrate/0.1% SDS at 50° C.    -   (b) 0.1×SSC at 65° C.    -   (c) 0.1×SSC, 0.5% SDS at 68° C.    -   (d) 0.1×SSC, 0.5% SDS, 50% formamide at 42° C.    -   (e) 0.2×SSC, 0.1% SDS at 42° C.    -   (f) 2×SSC at 65° C. (low-stringency condition).

Polypeptides having above-mentioned activity, i.e. conferring increasein yield, especially enhanced NUE and/or increased biomass production,as compared to a corresponding non-transformed wild type plant cell,plant or part thereof, derived from other organisms, can be encoded byother DNA sequences which hybridize to the sequences shown in table I,application no. 1, columns 5 and 7 under relaxed hybridizationconditions and which code on expression for peptides conferring increasein yield, especially the enhanced NUE efficiency and/or increasedbiomass production, as compared to a corresponding non-transformed wildtype plant cell, plant or part thereof.

Further, some applications have to be performed at low stringencyhybridization conditions, without any consequences for the specificityof the hybridization. For example, a Southern blot analysis of total DNAcould be probed with a nucleic acid molecule of the present inventionand washed at low stringency (55° C. in 2×SSPE, 0,1% SDS). Thehybridization analysis could reveal a simple pattern of only genesencoding polypeptides of the present invention or used in the process ofthe invention, e.g. having the herein-mentioned activity of enhancingthe NUE and/or increasing the biomass production as compared to acorresponding non-transformed wild type plant cell, plant or partthereof. A further example of such low-stringent hybridizationconditions is 4×SSC at 50° C. or hybridization with 30 to 40% formamideat 42° C. Such molecules comprise those which are fragments, analoguesor derivatives of the polypeptide of the invention or used in theprocess of the invention and differ, for example, by way of amino acidand/or nucleotide deletion(s), insertion(s), substitution (s),addition(s) and/or recombination (s) or any other modification(s) knownin the art either alone or in combination from the above-described aminoacid sequences or their underlying nucleotide sequence(s). However, itis preferred to use high stringency hybridization conditions.

Hybridization should advantageously be carried out with fragments of atleast 5, 10, 15, 20, 25, 30, 35 or 40 bp, advantageously at least 50,60, 70 or 80 bp, preferably at least 90, 100 or 110 bp. Most preferablyare fragments of at least 15, 20, 25 or 30 bp. Preferably are alsohybridizations with at least 100 by or 200, very especially preferablyat least 400 by in length. In an especially preferred embodiment, thehybridization should be carried out with the entire nucleic acidsequence with conditions described above.

The terms “fragment”, “fragment of a sequence” or “part of a sequence”mean a truncated sequence of the original sequence referred to. Thetruncated sequence (nucleic acid or protein sequence) can vary widely inlength; the minimum size being a sequence of sufficient size to providea sequence with at least a comparable function and/or activity of theoriginal sequence referred to or hybridizing with the nucleic acidmolecule of the invention or used in the process of the invention understringend conditions, while the maximum size is not critical. In someapplications, the maximum size usually is not substantially greater thanthat required to provide the desired activity and/or function(s) of theoriginal sequence.

Typically, the truncated amino acid sequence will range from about 5 toabout 310 amino acids in length. More typically, however, the sequencewill be a maximum of about 250 amino acids in length, preferably amaximum of about 200 or 100 amino acids. It is usually desirable toselect sequences of at least about 10, 12 or 15 amino acids, up to amaximum of about 20 or 25 amino acids.

The term “epitope” relates to specific immunoreactive sites within anantigen, also known as antigenic determinates. These epitopes can be alinear array of monomers in a polymeric composition—such as amino acidsin a protein—or consist of or comprise a more complex secondary ortertiary structure. Those of skill will recognize that immunogens (i.e.,substances capable of eliciting an immune response) are antigens;however, some antigen, such as haptens, are not immunogens but may bemade immunogenic by coupling to a carrier molecule. The term “antigen”includes references to a substance to which an antibody can be generatedand/or to which the antibody is specifically immunoreactive.

In one embodiment the present invention relates to a epitope of thepolypeptide of the present invention or used in the process of thepresent invention and confers an increased yield, especially an enhancedNUE and/or an increased biomass production, as compared to acorresponding non-transformed wild type plant cell, plant or partthereof.

The term “one or several amino acids” relates to at least one amino acidbut not more than that number of amino acids, which would result in ahomology of below 50% identity. Preferably, the identity is more than70% or 80%, more preferred are 85%, 90%, 91%, 92%, 93%, 94% or 95%, evenmore preferred are 96%, 97%, 98%, or 99% identity.

Further, the nucleic acid molecule of the invention comprises a nucleicacid molecule, which is a complement of one of the nucleotide sequencesof above mentioned nucleic acid molecules or a portion thereof. Anucleic acid molecule which is complementary to one of the nucleotidesequences shown in table I, application no. 1, columns 5 and 7 is onewhich is sufficiently complementary to one of the nucleotide sequencesshown in table I, columns 5 and 7 such that it can hybridize to one ofthe nucleotide sequences shown in table I, application no. 1, columns 5and 7, thereby forming a stable duplex. Preferably, the hybridization isperformed under stringent hybridization conditions. However, acomplement of one of the herein disclosed sequences is preferably asequence complement thereto according to the base pairing of nucleicacid molecules well known to the skilled person. For example, the basesA and G undergo base pairing with the bases T and U or C, resp. and visaversa. Modifications of the bases can influence the base-pairingpartner.

The nucleic acid molecule of the invention comprises a nucleotidesequence which is at least about 30%, 35%, 40% or 45%, preferably atleast about 50%, 55%, 60% or 65%, more preferably at least about 70%,80%, or 90%, and even more preferably at least about 95%, 97%, 98%, 99%or more homologous to a nucleotide sequence shown in table I,application no. 1, columns 5 and 7, or a portion thereof and preferablyhas above mentioned activity, in particular an increase in yield,especially having a NUE enhancing activity and/or biomass productionincreasing activity, after increasing the activity or an activity of agene product as shown in table II, application no. 1, column 3 by forexample expression either in the cytsol or in an organelle such as aplastid or mitochondria or both, preferably in plastids.

The nucleic acid molecule of the invention comprises a nucleotidesequence which hybridizes, preferably hybridizes under stringentconditions as defined herein, to one of the nucleotide sequences shownin table I, application no. 1, columns 5 and 7, or a portion thereof andencodes a protein having above-mentioned activity, e.g. conferring anincreased yield, especially an enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, plant or part thereof by for example expression either inthe cytsol or in an organelle such as a plastid or mitochondria or both,preferably in plastids, and optionally, the activity selected from thegroup consisting of 2-dehydro-3-deoxy-phosphoheptonate aldolase, 3-ketosterol reductase, 60S ribosomal protein, adeninephosphoribosyltransferase, adenylate kinase, alkyl hydroperoxidereductase, Alkyl/aryl-sulfatase, alpha-glucosidase, alpha-mannosidase,anaphase promoting complex (APC) subunit, antiviral adaptor protein,aromatic amino acid aminotransferase II, ARV1 protein,autophagy-specific phosphatidylinositol 3-kinase complex proteinsubunit, b0017-protein, B0165-protein, B1258-protein, B1267-protein,B1381-protein, b1933-protein, b2165-protein, b2238-protein,b2431-protein, B2646-protein, b2766-protein, b3120-protein, carnitineacetyltransferase, cell wall endo-beta-1,3-glucanase, chaperone, Chitinsynthase 3 complex protein, cholinephosphate cytidylyltransferase,chorismate mutase T prephenate dehydrogenase (bifunctional), clathrinassociated protein complex small subunit, component of the RAM signalingnetwork, cysteine transporter, cytochrome c oxidase subunit VIII,cytosolic catalase, cytosolic serine hydroxymethyltransferase,dihydroorotate dehydrogenase, dihydrosphingosine phosphate lyase,exoribonuclease, F1F0 ATP synthase beta subunit, Factor arrest protein,G protein coupled pheromone receptor receptor, gamma-glutamyl kinase,glucoamylase, glycerol-3-phosphate transporter subunit, glycinedecarboxylase, glycosyltransferase, golgi membrane exchange factorsubunit, golgi membrane protein, GPI-anchored cell wall protein,GTP-binding protein, helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-ketoreductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.

Moreover, the nucleic acid molecule of the invention can comprise only aportion of the coding region of one of the sequences shown in table I,application no. 1, columns 5 and 7, for example a fragment which can beused as a probe or primer or a fragment encoding a biologically activeportion of the polypeptide of the present invention or of a polypeptideused in the process of the present invention, i.e. havingabove-mentioned activity, e.g. conferring an increased yield, especiallyan enhanced NUE and/or biomass production, as compared to acorresponding non-transformed wild type plant cell, plant or partthereof f its activity is increased by for example expression either inthe cytsol or in an organelle such as a plastid or mitochondria or both,preferably in plastids. The nucleotide sequences determined from thecloning of the present protein-according-to-the-invention-encoding geneallows for the generation of probes and primers designed for use inidentifying and/or cloning its homologues in other cell types andorganisms. The probe/primer typically comprises substantially purifiedoligonucleotide. The oligonucleotide typically comprises a region ofnucleotide sequence that hybridizes under stringent conditions to atleast about 12, 15 preferably about 20 or 25, more preferably about 40,50 or 75 consecutive nucleotides of a sense strand of one of thesequences set forth, e.g., in table I, application no. 1, columns 5 and7, an anti-sense sequence of one of the sequences, e.g., set forth intable I, application no. 1, columns 5 and 7, or naturally occurringmutants thereof. Primers based on a nucleotide of invention can be usedin PCR reactions to clone homologues of the polypeptide of the inventionor of the polypeptide used in the process of the invention, e.g. as theprimers described in the examples of the present invention, e.g. asshown in the examples. A PCR with the primers shown in table III,application no. 1, column 7 will result in a fragment of the geneproduct as shown in table II, application no. 1, column 3.

Primer sets are interchangeable. The person skilled in the art knows tocombine said primers to result in the desired product, e.g. in a fulllength clone or a partial sequence. Probes based on the sequences of thenucleic acid molecule of the invention or used in the process of thepresent invention can be used to detect transcripts or genomic sequencesencoding the same or homologous proteins. The probe can further comprisea label group attached thereto, e.g. the label group can be aradioisotope, a fluorescent compound, an enzyme, or an enzyme co-factor.Such probes can be used as a part of a genomic marker test kit foridentifying cells which express an polypepetide of the invention or usedin the process of the present invention, such as by measuring a level ofan encoding nucleic acid molecule in a sample of cells, e.g., detectingmRNA levels or determining, whether a genomic gene comprising thesequence of the polynucleotide of the invention or used in the processof the present invention has been mutated or deleted.

The nucleic acid molecule of the invention encodes a polypeptide orportion thereof which includes an amino acid sequence which issufficiently homologous to the amino acid sequence shown in table II,application no. 1, columns 5 and 7 such that the protein or portionthereof maintains the ability to participate in increasing yield,especially in the enhancement of NUE and/or increase of biomassproduction, as compared to a corresponding non-transformed wild typeplant cell, plant or part thereof, in particular increasing the activityas mentioned above or as described in the examples in plants iscomprised.

As used herein, the language “sufficiently homologous” refers toproteins or portions thereof which have amino acid sequences whichinclude a minimum number of identical or equivalent amino acid residues(e.g., an amino acid residue which has a similar side chain as an aminoacid residue in one of the sequences of the polypeptide of the presentinvention) to an amino acid sequence shown in table II, application no.1, columns 5 and 7 such that the protein or portion thereof is able toparticipate in an increased yield, especially in the enhanced NUE and/orincrease of biomass production as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof. Forexamples having the activity of a protein as shown in table II,application no. 1, column 3 and as described herein.

In one embodiment, the nucleic acid molecule of the present inventioncomprises a nucleic acid that encodes a portion of the protein of thepresent invention. The protein is at least about 30%, 35%, 40%, 45% or50%, preferably at least about 55%, 60%, 65% or 70%, and more preferablyat least about 75%, 80%, 85%, 90%, 91%, 92%, 93% or 94% and mostpreferably at least about 95%, 97%, 98%, 99% or more homologous to anentire amino acid sequence of table II, application no. 1, columns 5 and7 and having above-mentioned activity, e.g. conferring an increasedyield, especially an enhanced NUE and/or increased biomass production,as compared to a corresponding non-transformed wild type plant cell,plant or part thereof by for example expression either in the cytosol orin an organelle such as a plastid or mitochondria or both, preferably inplastids.

Portions of proteins encoded by the nucleic acid molecule of theinvention are preferably biologically active, preferably havingabove-mentioned annotated activity, e.g. conferring an increased yield,especially an enhanced NUE and/or increase in biomass production, ascompared to a corresponding non-transformed wild type plant cell, plantor part thereof after increase of activity.

As mentioned herein, the term “biologically active portion” is intendedto include a portion, e.g., a domain/motif, that confers an increasedyield, especially an enhanced NUE and/or increase in biomass production,as compared to a corresponding non-transformed wild type plant cell,plant or part thereof or has an immunological activity such that it isbinds to an antibody binding specifically to the polypeptide of thepresent invention or a polypeptide used in the process of the presentinvention for an increased yield, especially an enhanced NUE and/orincreased biomass production, as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof.

The invention further relates to nucleic acid molecules that differ fromone of the nucleotide sequences shown in table I A, application no. 1,columns 5 and 7 (and portions thereof) due to degeneracy of the geneticcode and thus encode a polypeptide of the present invention, inparticular a polypeptide having above mentioned activity, e.g. as thatpolypeptides depicted by the sequence shown in table II, application no.1, columns 5 and 7 or the functional homologues. Advantageously, thenucleic acid molecule of the invention comprises, or in an otherembodiment has, a nucleotide sequence encoding a protein comprising, orin an other embodiment having, an amino acid sequence shown in table II,application no. 1, columns 5 and 7 or the functional homologues. In astill further embodiment, the nucleic acid molecule of the inventionencodes a full length protein which is substantially homologous to anamino acid sequence shown in table II, application no. 1, columns 5 and7 or the functional homologues. However, in a preferred embodiment, thenucleic acid molecule of the present invention does not consist of thesequence shown in table I, application no. 1, preferably table IA,columns 5 and 7.

In addition, it will be appreciated by those skilled in the art that DNAsequence polymorphisms that lead to changes in the amino acid sequencesmay exist within a population. Such genetic polymorphism in the geneencoding the polypeptide of the invention or comprising the nucleic acidmolecule of the invention may exist among individuals within apopulation due to natural variation.

As used herein, the terms “gene” and “recombinant gene” refer to nucleicacid molecules comprising an open reading frame encoding the polypeptideof the invention or comprising the nucleic acid molecule of theinvention or encoding the polypeptide used in the process of the presentinvention, preferably from a crop plant or from a microorganism usefulfor the method of the invention. Such natural variations can typicallyresult in 1 to 5% variance in the nucleotide sequence of the gene. Anyand all such nucleotide variations and resulting amino acidpolymorphisms in genes encoding a polypeptide of the invention orcomprising a the nucleic acid molecule of the invention that are theresult of natural variation and that do not alter the functionalactivity as described are intended to be within the scope of theinvention.

Nucleic acid molecules corresponding to natural variants homologues of anucleic acid molecule of the invention, which can also be a cDNA, can beisolated based on their homology to the nucleic acid molecules disclosedherein using the nucleic acid molecule of the invention, or a portionthereof, as a hybridization probe according to standard hybridizationtechniques under stringent hybridization conditions.

Accordingly, in another embodiment, a nucleic acid molecule of theinvention is at least 15, 20, 25 or 30 nucleotides in length.Preferably, it hybridizes under stringent conditions to a nucleic acidmolecule comprising a nucleotide sequence of the nucleic acid moleculeof the present invention or used in the process of the presentinvention, e.g. comprising the sequence shown in table I, applicationno. 1, columns 5 and 7. The nucleic acid molecule is preferably at least20, 30, 50, 100, 250 or more nucleotides in length.

The term “hybridizes under stringent conditions” is defined above. Inone embodiment, the term “hybridizes under stringent conditions” isintended to describe conditions for hybridization and washing underwhich nucleotide sequences at least 30%, 40%, 50% or 65% identical toeach other typically remain hybridized to each other. Preferably, theconditions are such that sequences at least about 70%, more preferablyat least about 75% or 80%, and even more preferably at least about 85%,90% or 95% or more identical to each other typically remain hybridizedto each other.

Preferably, nucleic acid molecule of the invention that hybridizes understringent conditions to a sequence shown in table I, application no. 1,columns 5 and 7 corresponds to a naturally-occurring nucleic acidmolecule of the invention. As used herein, a “naturally-occurring”nucleic acid molecule refers to an RNA or DNA molecule having anucleotide sequence that occurs in nature (e.g., encodes a naturalprotein). Preferably, the nucleic acid molecule encodes a naturalprotein having above-mentioned activity, e.g. conferring increasedyield, especially an enhanced NUE and/or increased biomass production,after increasing the expression or activity thereof or the activity of aprotein of the invention or used in the process of the invention by forexample expression the nucleic acid sequence of the gene product in thecytosol and/or in an organelle such as a plastid or mitochondria,preferably in plastids.

In addition to naturally-occurring variants of the sequences of thepolypeptide or nucleic acid molecule of the invention as well as of thepolypeptide or nucleic acid molecule used in the process of theinvention that may exist in the population, the skilled artisan willfurther appreciate that changes can be introduced by mutation into anucleotide sequence of the nucleic acid molecule encoding thepolypeptide of the invention or used in the process of the presentinvention, thereby leading to changes in the amino acid sequence of theencoded said polypeptide, without altering the functional ability of thepolypeptide, preferably not decreasing said activity.

For example, nucleotide substitutions leading to amino acidsubstitutions at “non-essential” amino acid residues can be made in asequence of the nucleic acid molecule of the invention or used in theprocess of the invention, e.g. shown in table I, application no. 1,columns 5 and 7.

A “non-essential” amino acid residue is a residue that can be alteredfrom the wild-type sequence of one without altering the activity of saidpolypeptide, whereas an “essential” amino acid residue is required foran activity as mentioned above, e.g. leading to an increased yield,especially an enhancement of NUE and/or increase of biomass production,as compared to a corresponding non-transformed wild type plant cell,plant or part thereof in an organism after an increase of activity ofthe polypeptide. Other amino acid residues, however, (e.g., those thatare not conserved or only semi-conserved in the domain having saidactivity) may not be essential for activity and thus are likely to beamenable to alteration without altering said activity.

Further, a person skilled in the art knows that the codon usage betweenorganisms can differ. Therefore, he may adapt the codon usage in thenucleic acid molecule of the present invention to the usage of theorganism or the cell compartment for example of the plastid ormitochondria in which the polynucleotide or polypeptide is expressed.

Accordingly, the invention relates to nucleic acid molecules encoding apolypeptide having above-mentioned activity, in an organism or a partthereof by for example expression either in the cytosol or in anorganelle such as a plastid or mitochondria or both, preferably inplastids that contain changes in amino acid residues that are notessential for said activity. Such polypeptides differ in amino acidsequence from a sequence contained in the sequences shown in table II,application no. 1, columns 5 and 7 yet retain said activity describedherein. The nucleic acid molecule can comprise a nucleotide sequenceencoding a polypeptide, wherein the polypeptide comprises an amino acidsequence at least about 50% identical to an amino acid sequence shown intable II, application no. 1, columns 5 and 7 and is capable ofparticipation in increasing yield, especially in the enhancement of NUEand/or increase of biomass production, as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof afterincreasing its activity, e.g. its expression by for example expressioneither in the cytosol or in an organelle such as a plastid ormitochondria or both, preferably in plastids. Preferably, the proteinencoded by the nucleic acid molecule is at least about 60% identical tothe sequence shown in table II, application no. 1, columns 5 and 7, morepreferably at least about 70% identical to one of the sequences shown intable II, application no. 1, columns 5 and 7, even more preferably atleast about 80%, 90%, 95% homologous to the sequence shown in table II,application no. 1, columns 5 and 7, and most preferably at least about96%, 97%, 98%, or 99% identical to the sequence shown in table II,application no. 1, columns 5 and 7.

To determine the percentage homology (=identity, herein usedinterchangeably) of two amino acid sequences or of two nucleic acidmolecules, the sequences are written one underneath the other for anoptimal comparison (for example gaps may be inserted into the sequenceof a protein or of a nucleic acid in order to generate an optimalalignment with the other protein or the other nucleic acid).

The amino acid residues or nucleic acid molecules at the correspondingamino acid positions or nucleotide positions are then compared. If aposition in one sequence is occupied by the same amino acid residue orthe same nucleic acid molecule as the corresponding position in theother sequence, the molecules are homologous at this position (i.e.amino acid or nucleic acid “homology” as used in the present contextcorresponds to amino acid or nucleic acid “identity”. The percentagehomology between the two sequences is a function of the number ofidentical positions shared by the sequences (i.e. % homology=number ofidentical positions/total number of positions×100). The terms “homology”and “identity” are thus to be considered as synonyms.

For the determination of the percentage homology (=identity) of two ormore amino acids or of two or more nucleotide sequences several computersoftware programs have been developed. The homology of two or moresequences can be calculated with for example the software fasta, whichpresently has been used in the version fasta 3 (W. R. Pearson and D. J.Lipman, PNAS 85, 2444 (1988); W. R. Pearson, Methods in Enzymology 183,63 (1990); W. R. Pearson and D. J. Lipman, PNAS 85, 2444 (1988); W. R.Pearson, Enzymology 183, 63 (1990)). Another useful program for thecalculation of homologies of different sequences is the standard blastprogram, which is included in the Biomax pedant software (Biomax,Munich, Federal Republic of Germany). This leads unfortunately sometimesto suboptimal results since blast does not always include completesequences of the subject and the query. Nevertheless as this program isvery efficient it can be used for the comparison of a huge number ofsequences. The following settings are typically used for such acomparisons of sequences:

-p Program Name [String]; -d Database [String]; default=nr; -i QueryFile [File In]; default=stdin; -e Expectation value (E) [Real];default=10.0; -m alignment view options: 0=pairwise; 1=query-anchoredshowing identities; 2=query-anchored no identities; 3=flatquery-anchored, show identities; 4=flat query-anchored, no identities;5=query-anchored no identities and blunt ends; 6=flat query-anchored, noidentities and blunt ends; 7=XML Blast output; 8=tabular; 9 tabular withcomment lines [Integer]; default=0; -o BLAST report Output File [FileOut] Optional; default=stdout; -F Filter query sequence (DUST withblastn, SEG with others) [String]; default=T; -G Cost to open a gap(zero invokes default behavior) [Integer]; default=0; -E Cost to extenda gap (zero invokes default behavior) [Integer]; default=0; -X X dropoffvalue for gapped alignment (in bits) (zero invokes default behavior);blastn 30, megablast 20, tblastx 0, all others 15 [Integer]; default=0;-I Show GI's in deflines [T/F]; default=F; -q Penalty for a nucleotidemismatch (blastn only) [Integer]; default=−3; -r Reward for a nucleotidematch (blastn only) [Integer]; default=1; -v Number of databasesequences to show one-line descriptions for (V) [Integer]; default=500;-b Number of database sequence to show alignments for (B) [Integer];default=250; -f Threshold for extending hits, default if zero; blastp11, blastn 0, blastx 12, tblastn 13; tblastx 13, megablast 0 [Integer];default=0; -g Perfom gapped alignment (not available with tblastx)[T/F]; default=T; -Q Query Genetic code to use [Integer]; default=1; -DDB Genetic code (for tblast[nx] only) [Integer]; default=1; -a Number ofprocessors to use [Integer]; default=1; -O SeqAlign file [File Out]Optional; -J Believe the query defline [T/F]; default=F; -M Matrix[String]; default=BLOSUM62; -W Word size, default if zero (blastn 11,megablast 28, all others 3) [Integer]; default=0; -z Effective length ofthe database (use zero for the real size) [Real]; default=0; -K Numberof best hits from a region to keep (off by default, if used a value of100 is recommended) [Integer]; default=0; -P 0 for multiple hit, 1 forsingle hit [Integer]; default=0; -Y Effective length of the search space(use zero for the real size) [Real]; default=0; -S Query strands tosearch against database (for blast[nx], and tblastx); 3 is both, 1 istop, 2 is bottom [Integer]; default=3; -T Produce HTML output [T/F];default=F; -I Restrict search of database to list of GI's [String]Optional; -U Use lower case filtering of FASTA sequence [T/F] Optional;default=F; -y X dropoff value for ungapped extensions in bits (0.0invokes default behavior); blastn 20, megablast 10, all others 7 [Real];default=0.0; -Z X dropoff value for final gapped alignment in bits (0.0invokes default behavior); blastn/megablast 50, tblastx 0, all others 25[Integer]; default=0; -R PSITBLASTN checkpoint file [File In] Optional;-n MegaBlast search [T/F]; default=F; -L Location on query sequence[String] Optional; -A Multiple Hits window size, default if zero(blastn/megablast 0, all others 40 [Integer]; default=0; -w Frame shiftpenalty (OOF algorithm for blastx) [Integer]; default=0; -t Length ofthe largest intron allowed in tblastn for linking HSPs (0 disableslinking) [Integer]; default=0.

Results of high quality are reached by using the algorithm of Needlemanand Wunsch or Smith and Waterman. Therefore programs based on saidalgorithms are preferred. Advantageously the comparisons of sequencescan be done with the program PileUp (J. Mol. Evolution., 25, 351 (1987),Higgins et al., CABIOS 5, 151 (1989)) or preferably with the programs“Gap” and “Needle”, which are both based on the algorithms of Needlemanand Wunsch (J. Mol. Biol. 48; 443 (1970)), and “BestFit”, which is basedon the algorithm of Smith and Waterman (Adv. Appl. Math. 2; 482 (1981)).“Gap” and “BestFit” are part of the GCG software-package (GeneticsComputer Group, 575 Science Drive, Madison, Wis., USA 53711 (1991);Altschul et al., (Nucleic Acids Res. 25, 3389 (1997)), “Needle” is partof the The European Molecular Biology Open Software Suite (EMBOSS)(Trends in Genetics 16 (6), 276 (2000)). Therefore preferably thecalculations to determine the percentages of sequence homology are donewith the programs “Gap” or “Needle” over the whole range of thesequences. The following standard adjustments for the comparison ofnucleic acid sequences were used for “Needle”: matrix: EDNAFULL,Gap_penalty: 10.0, Extend_penalty: 0.5. The following standardadjustments for the comparison of nucleic acid sequences were used for“Gap”: gap weight: 50, length weight: 3, average match: 10.000, averagemismatch: 0.000.

For example a sequence, which has 80% homology with sequence SEQ ID NO:38 at the nucleic acid level is understood as meaning a sequence which,upon comparison with the sequence SEQ ID NO: 38 by the above program“Needle” with the above parameter set, has a 80% homology.

Homology between two polypeptides is understood as meaning the identityof the amino acid sequence over in each case the entire sequence lengthwhich is calculated by comparison with the aid of the above program“Needle” using Matrix: EBLOSUM62, Gap_penalty: 8.0, Extend_penalty: 2.0.

For example a sequence which has a 80% homology with sequence SEQ ID NO39 at the protein level is understood as meaning a sequence which, uponcomparison with the sequence SEQ ID NO 39 by the above program “Needle”with the above parameter set, has a 80% homology.

Functional equivalents derived from the nucleic acid sequence as shownin table I, application no. 1, columns 5 and 7 according to theinvention by substitution, insertion or deletion have at least 30%, 35%,40%, 45% or 50%, preferably at least 55%, 60%, 65% or 70% by preferenceat least 80%, especially preferably at least 85% or 90%, 91%, 92%, 93%or 94%, very especially preferably at least 95%, 97%, 98% or 99%homology with one of the polypeptides as shown in table II, applicationno. 1, columns 5 and 7 according to the invention and encodepolypeptides having essentially the same properties as the polypeptideas shown in table II, application no. 1, columns 5 and 7.

Functional equivalents derived from one of the polypeptides as shown intable II, application no. 1, columns 5 and 7 according to the inventionby substitution, insertion or deletion have at least 30%, 35%, 40%, 45%or 50%, preferably at least 55%, 60%, 65% or 70% by preference at least80%, especially preferably at least 85% or 90%, 91%, 92%, 93% or 94%,very especially preferably at least 95%, 97%, 98% or 99% homology withone of the polypeptides as shown in table II, application no. 1, columns5 and 7 according to the invention and having essentially the sameproperties as the polypeptide as shown in table II, application no. 1,columns 5 and 7.

“Essentially the same properties” of a functional equivalent is aboveall understood as meaning that the functional equivalent has abovementioned activity, by for example expression either in the cytosol orin an organelle such as a plastid or mitochondria or both, preferably inplastids while increasing the amount of protein, activity or function ofsaid functional equivalent in an organism, e.g. a microorganism, a plantor plant tissue or animal tissue, plant or animal cells or a part of thesame.

A nucleic acid molecule encoding an homologous to a protein sequence oftable II, application no. 1, columns 5 and 7 can be created byintroducing one or more nucleotide substitutions, additions or deletionsinto a nucleotide sequence of the nucleic acid molecule of the presentinvention, in particular of table I, application no. 1, columns 5 and 7such that one or more amino acid substitutions, additions or deletionsare introduced into the encoded protein. Mutations can be introducedinto the encoding sequences of table I, application no. 1, columns 5 and7 by standard techniques, such as site-directed mutagenesis andPCR-mediated mutagenesis.

Preferably, conservative amino acid substitutions are made at one ormore predicted non-essential amino acid residues. A “conservative aminoacid substitution” is one in which the amino acid residue is replacedwith an amino acid residue having a similar side chain. Families ofamino acid residues having similar side chains have been defined in theart. These families include amino acids with basic side chains (e.g.,lysine, arginine, histidine), acidic side chains (e.g., aspartic acid,glutamic acid), uncharged polar side chains (e.g., glycine, asparagine,glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains(e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine,methionine, tryptophane), beta-branched side chains (e.g., threonine,valine, isoleucine) and aromatic side chains (e.g., tyrosine,phenylalanine, tryptophane, histidine).

Thus, a predicted nonessential amino acid residue in a polypeptide ofthe invention or a polypeptide used in the process of the invention ispreferably replaced with another amino acid residue from the samefamily. Alternatively, in another embodiment, mutations can beintroduced randomly along all or part of a coding sequence of a nucleicacid molecule of the invention or used in the process of the invention,such as by saturation mutagenesis, and the resultant mutants can bescreened for activity described herein to identify mutants that retainor even have increased above mentioned activity, e.g. conferring anenhanced NUE and/or increased biomass production as compared to acorresponding non-transformed wild type plant cell, plant or partthereof.

Following mutagenesis of one of the sequences as shown herein, theencoded protein can be expressed recombinant and the activity of theprotein can be determined using, for example, assays described herein(see Examples).

The highest homology of the nucleic acid molecule used in the processaccording to the invention was found for the following database entriesby Gap search.

Homologues of the nucleic acid sequences used, with the sequence shownin table I, application no. 1, columns 5 and 7, comprise also allelicvariants with at least approximately 30%, 35%, 40% or 45% homology, bypreference at least approximately 50%, 60% or 70%, more preferably atleast approximately 90%, 91%, 92%, 93%, 94% or 95% and even morepreferably at least approximately 96%, 97%, 98%, 99% or more homologywith one of the nucleotide sequences shown or the abovementioned derivednucleic acid sequences or their homologues, derivatives or analogues orparts of these. Allelic variants encompass in particular functionalvariants which can be obtained by deletion, insertion or substitution ofnucleotides from the sequences shown, preferably from table I,application no. 1, columns 5 and 7, or from the derived nucleic acidsequences, the intention being, however, that the enzyme activity or thebiological activity of the resulting proteins synthesized isadvantageously retained or increased.

In one embodiment of the present invention, the nucleic acid molecule ofthe invention or used in the process of the invention comprises thesequences shown in any of the table I, application no. 1, columns 5 and7. It is preferred that the nucleic acid molecule comprises as little aspossible other nucleotides not shown in any one of table I, applicationno. 1, columns 5 and 7. In one embodiment, the nucleic acid moleculecomprises less than 500, 400, 300, 200, 100, 90, 80, 70, 60, 50 or 40further nucleotides. In a further embodiment, the nucleic acid moleculecomprises less than 30, 20 or 10 further nucleotides. In one embodiment,the nucleic acid molecule use in the process of the invention isidentical to the sequences shown in table I, application no. 1, columns5 and 7.

Also preferred is that the nucleic acid molecule used in the process ofthe invention encodes a polypeptide comprising the sequence shown intable II, application no. 1, columns 5 and 7. In one embodiment, thenucleic acid molecule encodes less than 150, 130, 100, 80, 60, 50, 40 or30 further amino acids. In a further embodiment, the encoded polypeptidecomprises less than 20, 15, 10, 9, 8, 7, 6 or 5 further amino acids. Inone embodiment used in the inventive process, the encoded polypeptide isidentical to the sequences shown in table II, application no. 1, columns5 and 7.

In one embodiment, the nucleic acid molecule of the invention or used inthe process encodes a polypeptide comprising the sequence shown in tableII, application no. 1, columns 5 and 7 comprises less than 100 furthernucleotides. In a further embodiment, said nucleic acid moleculecomprises less than 30 further nucleotides. In one embodiment, thenucleic acid molecule used in the process is identical to a codingsequence of the sequences shown in table I, application no. 1, columns 5and 7.

Polypeptides (=proteins), which still have the essential biological orenzymatic activity of the polypeptide of the present inventionconferring an increased yield, especially an enhanced NUE and/orincreased biomass production, as compared to a correspondingnon-transformed wild type plant cell, plant or part thereof i.e. whoseactivity is essentially not reduced, are polypeptides with at least 10%or 20%, by preference 30% or 40%, especially preferably 50% or 60%, veryespecially preferably 80% or 90 or more of the wild type biologicalactivity or enzyme activity, advantageously, the activity is essentiallynot reduced in comparison with the activity of a polypeptide shown intable II, application no. 1, columns 5 and 7 expressed under identicalconditions.

Homologues of table I, application no. 1, columns 5 and 7 or of thederived sequences of table II, columns 5 and 7 also mean truncatedsequences, cDNA, single-stranded DNA or RNA of the coding and noncodingDNA sequence. Homologues of said sequences are also understood asmeaning derivatives, which comprise noncoding regions such as, forexample, UTRs, terminators, enhancers or promoter variants. Thepromoters upstream of the nucleotide sequences stated can be modified byone or more nucleotide substitution(s), insertion(s) and/or deletion(s)without, however, interfering with the functionality or activity eitherof the promoters, the open reading frame (=ORF) or with the3′-regulatory region such as terminators or other 3′-regulatory regions,which are far away from the ORF. It is furthermore possible that theactivity of the promoters is increased by modification of theirsequence, or that they are replaced completely by more active promoters,even promoters from heterologous organisms. Appropriate promoters areknown to the person skilled in the art and are mentioned herein below.

In addition to the nucleic acid molecules encoding the NUERPs describedabove, another aspect of the invention pertains to negative regulatorsof the activity of a nucleic acid molecules selected from the groupaccording to table I, application no. 1, column 5 and/or 7, preferablycolumn 7. Antisense polynucleotides thereto are thought to inhibit thedownregulating activity of those negative regulators by specificallybinding the target polynucleotide and interfering with transcription,splicing, transport, translation, and/or stability of the targetpolynucleotide. Methods are described in the prior art for targeting theantisense polynucleotide to the chromosomal DNA, to a primary RNAtranscript, or to a processed mRNA. Preferably, the target regionsinclude splice sites, translation initiation codons, translationtermination codons, and other sequences within the open reading frame.

The term “antisense,” for the purposes of the invention, refers to anucleic acid comprising a polynucleotide that is sufficientlycomplementary to all or a portion of a gene, primary transcript, orprocessed mRNA, so as to interfere with expression of the endogenousgene. “Complementary” polynucleotides are those that are capable of basepairing according to the standard Watson-Crick complementarity rules.Specifically, purines will base pair with pyrimidines to form acombination of guanine paired with cytosine (G:C) and adenine pairedwith either thymine (A:T) in the case of DNA, or adenine paired withuracil (A:U) in the case of RNA. It is understood that twopolynucleotides may hybridize to each other even if they are notcompletely complementary to each other, provided that each has at leastone region that is substantially complementary to the other. The term“antisense nucleic acid” includes single stranded RNA as well asdouble-stranded DNA expression cassettes that can be transcribed toproduce an antisense RNA. “Active” antisense nucleic acids are antisenseRNA molecules that are capable of selectively hybridizing with anegative regulator of the activity of a nucleic acid molecules encodinga polypeptide having at least 80% sequence identity with the polypeptideselected from the group according to table II, application no. 1, column5 and/or 7, preferably column 7.

The antisense nucleic acid can be complementary to an entire negativeregulator strand, or to only a portion thereof. In an embodiment, theantisense nucleic acid molecule is antisense to a “noncoding region” ofthe coding strand of a nucleotide sequence encoding a NUERP. The term“noncoding region” refers to 5′ and 3′ sequences that flank the codingregion that are not translated into amino acids (i.e., also referred toas 5′ and 3′ untranslated regions). The antisense nucleic acid moleculecan be complementary to only a portion of the noncoding region of NUERPmRNA. For example, the antisense oligonucleotide can be complementary tothe region surrounding the translation start site of NUERP mRNA. Anantisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25,30, 35, 40, 45 or 50 nucleotides in length. Typically, the anti-sensemolecules of the present invention comprise an RNA having 60-100%sequence identity with at least 14 consecutive nucleotides of anoncoding region of one of the nucleic acid of table I. Preferably, thesequence identity will be at least 70%, more preferably at least 75%,80%, 85%, 90%, 95%, 98% and most preferably 99%.

An antisense nucleic acid of the invention can be constructed usingchemical synthesis and enzymatic ligation reactions using proceduresknown in the art. For example, an antisense nucleic acid (e.g., anantisense oligonucleotide) can be chemically synthesized using naturallyoccurring nucleotides or variously modified nucleotides designed toincrease the biological stability of the molecules or to increase thephysical stability of the duplex formed between the antisense and sensenucleic acids, e.g., phosphorothioate derivatives and acridinesubstituted nucleotides can be used. Examples of modified nucleotideswhich can be used to generate the antisense nucleic acid include5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil,hypoxanthine, xanthine, 4-acetylcytosine,5-(carboxyhydroxylmethyl)-uracil,5-carboxymethylaminomethyl-2-thiouridine,5-carboxymethylaminomethyluracil, dihydrouracil,beta-D-galactosylqueosine, inosine, N6-isopentenyladenine,1-methylguanine, 1-methylinosine, 2,2-dimethylguanine, 2-methyladenine,2-methylguanine, 3-methylcytosine, 5-methylcytosine, N6-adenine,7-methylguanine, 5-methylaminomethyluracil,5-methoxyaminomethyl-2-thiouracil, beta-D-mannosylqueosine,5′-methoxycarboxymethyluracil, 5-methoxyuracil,2-methylthio-N6-isopentenyladenine, uracil-5-oxyacetic acid (v),wybutoxosine, pseudouracil, queosine, 2-thiocytosine,5-methyl-2-thiouracil, 2-thiouracil, 4-thiouracil, 5-methyluracil,uracil-5-oxyacetic acid methylester, 5-methyl-2-thiouracil,3-(3-amino-3-N-2-carboxypropyl)-uracil, acp3 and 2,6-diaminopurine.Alternatively, the antisense nucleic acid can be produced biologicallyusing an expression vector into which a nucleic acid has been subclonedin an antisense orientation (i.e., RNA transcribed from the insertednucleic acid will be of an antisense orientation to a target nucleicacid of interest, described further in the following subsection).

In yet another embodiment, the antisense nucleic acid molecule of theinvention is an alpha-anomeric nucleic acid molecule. An alpha-anomericnucleic acid molecule forms specific double-stranded hybrids withcomplementary RNA in which, contrary to the usual b-units, the strandsrun parallel to each other (Gaultier et al., Nucleic Acids. Res. 15,6625 (1987)). The antisense nucleic acid molecule can also comprise a2′-o-methylribonucleotide (Inoue et al., Nucleic Acids Res. 15, 6131(1987)) or a chimeric RNA-DNA analogue (Inoue et al., FEBS Lett. 215,327 (1987)).

The antisense nucleic acid molecules of the invention are typicallyadministered to a cell or generated in situ such that they hybridizewith or bind to cellular mRNA and/or genomic DNA. The hybridization canbe by conventional nucleotide complementarity to form a stable duplex,or, for example, in the case of an antisense nucleic acid molecule whichbinds to DNA duplexes, through specific interactions in the major grooveof the double helix. The antisense molecule can be modified such that itspecifically binds to a receptor or an antigen expressed on a selectedcell surface, e.g., by linking the antisense nucleic acid molecule to apeptide or an antibody which binds to a cell surface receptor orantigen. The antisense nucleic acid molecule can also be delivered tocells using the vectors described herein. To achieve sufficientintracellular concentrations of the antisense molecules, vectorconstructs in which the antisense nucleic acid molecule is placed underthe control of a strong prokaryotic, viral, or eukaryotic (includingplant) promoter are preferred.

As an alternative to antisense polynucleotides, ribozymes, sensepolynucleotides, or double stranded RNA (dsRNA) can be used to reduceexpression of a NUERP polypeptide. By “ribozyme” is meant a catalyticRNA-based enzyme with ribonuclease activity which is capable of cleavinga single-stranded nucleic acid, such as an mRNA, to which it has acomplementary region. Ribozymes (e.g., hammerhead ribozymes described inHaselhoff and Gerlach, Nature 334, 585 (1988)) can be used tocatalytically cleave NUERP mRNA transcripts to thereby inhibittranslation of NUERP mRNA. A ribozyme having specificity for aNUERP-encoding nucleic acid can be designed based upon the nucleotidesequence of a NUERP cDNA, as disclosed herein or on the basis of aheterologous sequence to be isolated according to methods taught in thisinvention. For example, a derivative of a Tetrahymena L-19 IVS RNA canbe constructed in which the nucleotide sequence of the active site iscomplementary to the nucleotide sequence to be cleaved in aNUERP-encoding mRNA. See, e.g. U.S. Pat. Nos. 4,987,071 and 5,116,742 toCech et al. Alternatively, NUERP mRNA can be used to select a catalyticRNA having a specific ribonuclease activity from a pool of RNAmolecules. See, e.g. Bartel D., and Szostak J.W., Science 261, 1411(1993). In preferred embodiments, the ribozyme will contain a portionhaving at least 7, 8, 9, 10, 12, 14, 16, 18 or 20 nucleotides, and morepreferably 7 or 8 nucleotides, that have 100% complementarity to aportion of the target RNA. Methods for making ribozymes are known tothose skilled in the art. See, e.g. U.S. Pat. Nos. 6,025,167, 5,773,260and 5,496,698.

The term “dsRNA,” as used herein, refers to RNA hybrids comprising twostrands of RNA. The dsRNAs can be linear or circular in structure. In apreferred embodiment, dsRNA is specific for a polynucleotide encodingeither the polypeptide according to table II or a polypeptide having atleast 70% sequence identity with a polypeptide according to table II.The hybridizing RNAs may be substantially or completely complementary.By “substantially complementary,” is meant that when the two hybridizingRNAs are optimally aligned using the BLAST program as described above,the hybridizing portions are at least 95% complementary. Preferably, thedsRNA will be at least 100 base pairs in length. Typically, thehybridizing RNAs will be of identical length with no over hanging 5′ or3′ ends and no gaps. However, dsRNAs having 5′ or 3′ overhangs of up to100 nucleotides may be used in the methods of the invention.

The dsRNA may comprise ribonucleotides or ribonucleotide analogs, suchas 2′-O-methyl ribosyl residues, or combinations thereof. See, e.g. U.S.Pat. Nos. 4,130,641 and 4,024,222. A dsRNA polyriboinosinicacid:polyribocytidylic acid is described in U.S. Pat. No. 4,283,393.Methods for making and using dsRNA are known in the art. One methodcomprises the simultaneous transcription of two complementary DNAstrands, either in vivo, or in a single in vitro reaction mixture. See,e.g. U.S. Pat. No. 5,795,715. In one embodiment, dsRNA can be introducedinto a plant or plant cell directly by standard transformationprocedures. Alternatively, dsRNA can be expressed in a plant cell bytranscribing two complementary RNAs.

Other methods for the inhibition of endogenous gene expression, such astriple helix formation (Moser et al., Science 238, 645 (1987), andCooney et al., Science 241, 456 (1988)) and cosuppression (Napoli etal., The Plant Cell 2,279, 1990,) are known in the art. Partial andfull-length cDNAs have been used for the cosuppression of endogenousplant genes. See, e.g. U.S. Pat. Nos. 4,801,340, 5,034,323, 5,231,020,and 5,283,184; Van der Kroll et al., The Plant Cell 2, 291, (1990);Smith et al., Mol. Gen. Genetics 224, 477 (1990), and Napoli et al., ThePlant Cell 2, 279 (1990).

For sense suppression, it is believed that introduction of a sensepolynucleotide blocks transcription of the corresponding target gene.The sense polynucleotide will have at least 65% sequence identity withthe target plant gene or RNA. Preferably, the percent identity is atleast 80%, 90%, 95% or more. The introduced sense polynucleotide neednot be full length relative to the target gene or transcript.Preferably, the sense polynucleotide will have at least 65% sequenceidentity with at least 100 consecutive nucleotides of one of the nucleicacids as depicted in table I, application no. 1. The regions of identitycan comprise introns and/or exons and untranslated regions. Theintroduced sense polynucleotide may be present in the plant celltransiently, or may be stably integrated into a plant chromosome orextrachromosomal replicon.

Further, object of the invention is an expression vector comprising anucleic acid molecule comprising a nucleic acid molecule selected fromthe group consisting of:

-   (a) a nucleic acid molecule encoding the polypeptide shown in column    5 or 7 of table II, application no. 1;-   (b) a nucleic acid molecule shown in column 5 or 7 of table I,    application no. 1;-   (c) a nucleic acid molecule, which, as a result of the degeneracy of    the genetic code, can be derived from a polypeptide sequence    depicted in column 5 or 7 of table II, application no. 1, and    confers an increased yield, especially an enhanced NUE and/or    increased biomass production, as compared to a corresponding    non-transformed wild type plant cell, a plant or a part thereof;-   (d) a nucleic acid molecule having at least 30% identity, preferably    at least 40%, 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%,    99%, 99.5% with the nucleic acid molecule sequence of a    polynucleotide comprising the nucleic acid molecule shown in column    5 or 7 of table I, application no. 1, and confers an increased    yield, especially an enhanced NUE and/or increased biomass    production, as compared to a corresponding non-transformed wild type    plant cell, a plant or a part thereof;-   (e) a nucleic acid molecule encoding a polypeptide having at least    30% identity, preferably at least 40%, 50%, 60%, 70%, 75%, 80%, 85%,    90%, 95%, 96%, 97%, 98%, 99%, 99.5%, with the amino acid sequence of    the polypeptide encoded by the nucleic acid molecule of (a),    (b), (c) or (d) and having the activity represented by a nucleic    acid molecule comprising a polynucleotide as depicted in column 5 of    table I, application no. 1, and confers an increased yield,    especially an enhanced NUE and/or increased biomass production, as    compared to a corresponding non-transformed wild type plant cell, a    plant or a part thereof;-   (f) nucleic acid molecule which hybridizes with a nucleic acid    molecule of (a), (b), (c), (d) or (e) under stringent hybridization    conditions and confers an increased yield, especially an enhanced    NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, a plant or a    part thereof;-   (g) a nucleic acid molecule encoding a polypeptide which can be    isolated with the aid of monoclonal or polyclonal antibodies made    against a polypeptide encoded by one of the nucleic acid molecules    of (a), (b), (c), (d), (e) or (f) and having the activity    represented by the nucleic acid molecule comprising a polynucleotide    as depicted in column 5 of table I, application no. 1;-   (h) a nucleic acid molecule encoding a polypeptide comprising the    consensus sequence or one or more polypeptide motifs as shown in    column 7 of table IV, application no. 1, and preferably having the    activity represented by a protein molecule comprising a polypeptide    as depicted in column 5 of table II or IV, application no. 1,-   (i) a nucleic acid molecule encoding a polypeptide having the    activity represented by a protein as depicted in column 5 of table    II, application no. 1, and confers an increased yield, especially an    enhanced NUE and/or increased biomass production, as compared to a    corresponding non-transformed wild type plant cell, a plant or a    part thereof;-   (j) nucleic acid molecule which comprises a polynucleotide, which is    obtained by amplifying a cDNA library or a genomic library using the    primers in column 7 of table III, application no. 1, (which ion a    special embodiment do not start at their 5′-end with the nucleotides    ATA and) preferably having the activity represented by a protein    molecule comprising a polypeptide as depicted in column 5 of table    II or IV, application no. 1;    and-   (k) a nucleic acid molecule which is obtainable by screening a    suitable nucleic acid library, especially a cDNA library and/or a    genomic library, under stringent hybridization conditions with a    probe comprising a complementary sequence of a nucleic acid molecule    of (a) or (b) or with a fragment thereof, having at least 15 nt,    preferably 20 nt, 30 nt, 50 nt, 100 nt, 200 nt, 500 nt, 750 or 1000    nt of a nucleic acid molecule complementary to a nucleic acid    molecule sequence characterized in (a) to (e) and encoding a    polypeptide having the activity represented by a protein comprising    a polypeptide as depicted in column 5 of table II, application no.

The invention further provides an isolated recombinant expression vectorcomprising a NUERP encoding nucleic acid as described above, whereinexpression of the vector or NUERP encoding nucleic acid, respectively ina host cell results in enhanced NUE as compared to the correspondingnon-transformed wild type of the host cell. As used herein, the term“vector” refers to a nucleic acid molecule capable of transportinganother nucleic acid to which it has been linked. One type of vector isa “plasmid”, which refers to a circular double stranded DNA loop intowhich additional DNA segments can be ligated. Another type of vector isa viral vector, wherein additional DNA segments can be ligated into theviral genome. Further types of vectors can be linearized nucleic acidsequences, such as transposons, which are pieces of DNA which can copyand insert themselves. There have been 2 types of transposons found:simple transposons, known as Insertion Sequences and compositetransposons, which can have several genes as well as the genes that arerequired for transposition.

Certain vectors are capable of autonomous replication in a host cellinto which they are introduced (e.g., bacterial vectors having abacterial origin of replication and episomal mammalian vectors). Othervectors (e.g., non-episomal mammalian vectors) are integrated into thegenome of a host cell upon introduction into the host cell, and therebyare replicated along with the host genome. Moreover, certain vectors arecapable of directing the expression of genes to which they areoperatively linked. Such vectors are referred to herein as “expressionvectors”. In general, expression vectors of utility in recombinant DNAtechniques are often in the form of plasmids. In the presentspecification, “plasmid” and “vector” can be used interchangeably as theplasmid is the most commonly used form of vector. However, the inventionis intended to include such other forms of expression vectors, such asviral vectors (e.g., replication defective retroviruses, adenovirusesand adeno-associated viruses), which serve equivalent functions.

A plant expression cassette preferably contains regulatory sequencescapable of driving gene expression in plant cells and operably linked sothat each sequence can fulfill its function, for example, termination oftranscription by polyadenylation signals. Preferred polyadenylationsignals are those originating from Agrobacterium tumefaciens T-DNA suchas the gene 3 known as octopine synthase of the Ti-plasmid pTiACH5(Gielen et al., EMBO J. 3, 835 1(984)) or functional equivalents thereofbut also all other terminators functionally active in plants aresuitable.

As plant gene expression is very often not limited on transcriptionallevels, a plant expression cassette preferably contains other operablylinked sequences like translational enhancers such as theoverdrive-sequence containing the 5″-untranslated leader sequence fromtobacco mosaic virus enhancing the protein per RNA ratio (Gallie et al.,Nucl. Acids Research 15, 8693 (1987)).

Plant gene expression has to be operably linked to an appropriatepromoter conferring gene expression in a timely, cell or tissue specificmanner. Preferred are promoters driving constitutive expression (Benfeyet al., EMBO J. 8, 2195 (1989)) like those derived from plant viruseslike the 35S CaMV (Franck et al., Cell 21, 285 (1980)), the 19S CaMV(see also U.S. Pat. No. 5,352,605 and PCT Application No. WO 84/02913)or plant promoters like those from Rubisco small subunit described inU.S. Pat. No. 4,962,028.

Additional advantageous regulatory sequences are, for example, includedin the plant promoters such as CaMV/35S (Franck et al., Cell 21 285(1980)), PRP1 (Ward et al., Plant. Mol. Biol. 22, 361 (1993)), SSU, OCS,lib4, usp, STLS1, B33, LEB4, nos, ubiquitin, napin or phaseolinpromoter. Also advantageous in this connection are inducible promoterssuch as the promoters described in EP 388 186 (benzyl sulfonamideinducible), Gatz et al., Plant J. 2, 397 (1992) (tetracyclin inducible),EP-A-0 335 528 (abscisic acid inducible) or WO 93/21334 (ethanol orcyclohexenol inducible). Additional useful plant promoters are thecytosolic FBPase promotor or ST-LSI promoter of potato (Stockhaus etal., EMBO J. 8, 2445 (1989)), the phosphorybosyl phyrophoshate amidotransferase promoter of Glycine max (gene bank accession No. U87999) orthe noden specific promoter described in EP-A-0 249 676. Additionalparticularly advantageous promoters are seed specific promoters whichcan be used for monocotyledones or dicotyledones and are described inU.S. Pat. No. 5,608,152 (napin promoter from rapeseed), WO 98/45461(phaseolin promoter from Arabidopsis), U.S. Pat. No. 5,504,200(phaseolin promoter from Phaseolus vulgaris), WO 91/13980 (Bce4 promoterfrom Brassica) and Baeumlein et al., Plant J., 2 (2), 233 (1992) (LEB4promoter from leguminosa). Said promoters are useful in dicotyledones.The following promoters are useful for example in monokcotyledonesIpt-2- or Ipt-1-promoter from barley (WO 95/15389 and WO 95/23230) orhordein promoter from barley. Other useful promoters are described in WO99/16890.

It is possible in principle to use all natural promoters with theirregulatory sequences like those mentioned above for the novel process.It is also possible and advantageous in addition to use syntheticpromoters.

The gene construct may also comprise further genes which are to beinserted into the organisms and which are for example involved in stressresistance and biomass production increase. It is possible andadvantageous to insert and express in host organisms regulatory genessuch as genes for inducers, repressors or enzymes which intervene bytheir enzymatic activity in the regulation, or one or more or all genesof a biosynthetic pathway. These genes can be heterologous or homologousin origin. The inserted genes may have their own promotor or else beunder the control of same promoter as the sequences of the nucleic acidof table I or their homologs. The gene construct advantageouslycomprises, for expression of the other genes present, additionally 3′and/or 5′ terminal regulatory sequences to enhance expression, which areselected for optimal expression depending on the selected host organismand gene or genes.

These regulatory sequences are intended to make specific expression ofthe genes and protein expression possible as mentioned above. This maymean, depending on the host organism, for example that the gene isexpressed or overexpressed only after induction, or that it isimmediately expressed and/or overexpressed.

The regulatory sequences or factors may moreover preferably have abeneficial effect on expression of the introduced genes, and thusincrease it. It is possible in this way for the regulatory elements tobe enhanced advantageously at the transcription level by using strongtranscription signals such as promoters and/or enhancers. However, inaddition, it is also possible to enhance translation by, for example,improving the stability of the mRNA.

Other preferred sequences for use in plant gene expression cassettes aretargeting-sequences necessary to direct the gene product in itsappropriate cell compartment (for review see Kermode, Crit. Rev. PlantSci. 15 (4), 285 (1996) and references cited therein) such as thevacuole, the nucleus, all types of plastids like amyloplasts,chloroplasts, chromoplasts, the extracellular space, mitochondria, theendoplasmic reticulum, oil bodies, peroxisomes and other compartments ofplant cells. Plant gene expression can also be facilitated via aninducible promoter (for review see Gatz, Annu. Rev. Plant Physiol. PlantMol. Biol. 48, 89 (1997)). Chemically inducible promoters are especiallysuitable if gene expression is wanted to occur in a time specificmanner.

Table VI lists several examples of promoters that may be used toregulate transcription of the NUE related protein nucleic acid codingsequences.

TABLE VI Examples of tissue-specific and inducible promoters in plantsExpression Reference Cor78 - Cold, drought, salt, Ishitani, et al.,Plant Cell 9, 1935 (1997), ABA, wounding-inducible Yamaguchi-Shinozakiand Shinozaki, Plant Cell 6, 251 (1994) Rci2A - Cold, dehydration- Capelet al., Plant Physiol 115, 569 (1997) inducible Rd22 - Drought, saltYamaguchi-Shinozaki and Shinozaki, Mol. Gen. Genet 238, 17 (1993)Cor15A - Cold, dehydration, Baker et al., Plant Mol. Biol. 24, ABA 701(1994) GH3- Auxin inducible Liu et al., Plant Cell 6, 645 (1994)ARSK1-Root, salt inducible Hwang and Goodman, Plant J. 8, 37 (1995)PtxA - Root, salt inducible GenBank accession X67427 SbHRGP3 - Rootspecific Ahn et al., Plant Cell 8, 1477 (1998). KST1 - Guard cellspecific Plesch et al., Plant Journal. 28(4): 455- (2001) KAT1 - Guardcell specific Plesch et al., Gene 249, 83 (2000), Nakamura et al., PlantPhysiol. 109, 371 (1995) salicylic acid inducible PCT Application No. WO95/19443 tetracycline inducible Gatz et al. Plant J. 2, 397 (1992)Ethanol inducible PCT Application No. WO 93/21334 Pathogen induciblePRP1 Ward et al., Plant. Mol. Biol. 22, 361 -(1993) Heat inducible hsp80U.S. Pat. No. 5,187,267 Cold inducible alpha-amylase PCT Application No.WO 96/12814 Wound-inducible pinII European Patent No. 375 091 RD29A -salt-inducible Yamaguchi-Shinozalei et al. Mol. Gen. Genet. 236, 331(1993) Plastid-specific viral RNA- PCT Application No. WO 95/16783, PCTpolymerase Application WO 97/06250

Other promotors, e.g. superpromotor (Ni et al., Plant Journal 7, 661(1995)), Ubiquitin promotor (Callis et al., J. Biol. Chem., 265, 12486(1990); U.S. Pat. No. 5,510,474; U.S. Pat. No. 6,020,190; Kawalleck etal., Plant. Molecular Biology, 21, 673 (1993)) or 34S promotor (GenBankAccession numbers M59930 and X16673) were similar useful for the presentinvention and are known to a person skilled in the art.

Developmental stage-preferred promoters are preferentially expressed atcertain stages of development. Tissue and organ preferred promotersinclude those that are preferentially expressed in certain tissues ororgans, such as leaves, roots, seeds, or xylem. Examples of tissuepreferred and organ preferred promoters include, but are not limited tofruit-preferred, ovule-preferred, male tissue-preferred, seed-preferred,integument-preferred, tuber-preferred, stalk-preferred,pericarp-preferred, and leaf-preferred, stigma-preferred,pollen-preferred, anther-preferred, a petal-preferred, sepal-preferred,pedicel-preferred, silique-preferred, stem-preferred, root-preferredpromoters, and the like. Seed preferred promoters are preferentiallyexpressed during seed development and/or germination. For example, seedpreferred promoters can be embryo-preferred, endosperm preferred, andseed coat-preferred. See Thompson et al., BioEssays 10, 108 (1989).Examples of seed preferred promoters include, but are not limited to,cellulose synthase (celA), Cim1, gamma-zein, globulin-1, maize 19 kDzein (cZ19B1), and the like.

Other promoters useful in the expression cassettes of the inventioninclude, but are not limited to, the major chlorophyll a/b bindingprotein promoter, histone promoters, the Ap3 promoter, the β-conglycinpromoter, the napin promoter, the soybean lectin promoter, the maize 15kD zein promoter, the 22 kD zein promoter, the 27 kD zein promoter, theg-zein promoter, the waxy, shrunken 1, shrunken 2 and bronze promoters,the Zm13 promoter (U.S. Pat. No. 5,086,169), the maize polygalacturonasepromoters (PG) (U.S. Pat. Nos. 5,412,085 and 5,545,546), and the SGB6promoter (U.S. Pat. No. 5,470,359), as well as synthetic or othernatural promoters.

Additional flexibility in controlling heterologous gene expression inplants may be obtained by using DNA binding domains and responseelements from heterologous sources (i.e., DNA binding domains fromnon-plant sources). An example of such a heterologous DNA binding domainis the LexA DNA binding domain (Brent and Ptashne, Cell 43, 729 (1985)).

The invention further provides a recombinant expression vectorcomprising a NUERP DNA molecule of the invention cloned into theexpression vector in an antisense orientation. That is, the DNA moleculeis operatively linked to a regulatory sequence in a manner that allowsfor expression (by transcription of the DNA molecule) of an RNA moleculethat is antisense to a NUERP mRNA. Regulatory sequences operativelylinked to a nucleic acid molecule cloned in the antisense orientationcan be chosen which direct the continuous expression of the antisenseRNA molecule in a variety of cell types. For instance, viral promotersand/or enhancers, or regulatory sequences can be chosen which directconstitutive, tissue specific, or cell type specific expression ofantisense RNA. The antisense expression vector can be in the form of arecombinant plasmid, phagemid, or attenuated virus wherein antisensenucleic acids are produced under the control of a high efficiencyregulatory region. The activity of the regulatory region can bedetermined by the cell type into which the vector is introduced. For adiscussion of the regulation of gene expression using antisense genes,see Weintraub H. et al., Reviews—Trends in Genetics, Vol. 1(1), 23(1986) and Mol et al., FEBS Letters 268, 427 (1990).

Another aspect of the invention pertains to isolated NUERPs, andbiologically active portions thereof. An “isolated” or “purified”polypeptide or biologically active portion thereof is free of some ofthe cellular material when produced by recombinant DNA techniques, orchemical precursors or other chemicals when chemically synthesized. Thelanguage “substantially free of cellular material” includes preparationsof NUERP in which the polypeptide is separated from some of the cellularcomponents of the cells in which it is naturally or recombinantlyproduced. In one embodiment, the language “substantially free ofcellular material” includes preparations of a NUERP having less thanabout 30% (by dry weight) of non-NUERP material (also referred to hereinas a “contaminating polypeptide”), more preferably less than about 20%of non-NUERP material, still more preferably less than about 10% ofnon-NUERP material, and most preferably less than about 5% non-NUERPmaterial.

When the NUERP or biologically active portion thereof is recombinantlyproduced, it is also preferably substantially free of culture medium,i.e., culture medium represents less than about 20%, more preferablyless than about 10%, and most preferably less than about 5% of thevolume of the polypeptide preparation. The language “substantially freeof chemical precursors or other chemicals” includes preparations ofNUERP in which the polypeptide is separated from chemical precursors orother chemicals that are involved in the synthesis of the polypeptide.In one embodiment, the language “substantially free of chemicalprecursors or other chemicals” includes preparations of a NUERP havingless than about 30% (by dry weight) of chemical precursors or non-NUERPchemicals, more preferably less than about 20% chemical precursors ornon-NUERP chemicals, still more preferably less than about 10% chemicalprecursors or non-NUERP chemicals, and most preferably less than about5% chemical precursors or non-NUERP chemicals. In preferred embodiments,isolated polypeptides, or biologically active portions thereof, lackcontaminating polypeptides from the same organism from which the NUERPis derived. Typically, such polypeptides are produced by recombinantexpression of, for example, a Saccharomyces cerevisiae, E. coli orBrassica napus, Glycine max, Zea mays or Oryza sativa NUERP, in anmicroorganism like Saccharomyces cerevisiae, E. coli, C. glutamicum,ciliates, algae, fungi or plants, provided that the polypeptide isrecombinant expressed in an organism being different to the originalorganism.

The nucleic acid molecules, polypeptides, polypeptide homologs, fusionpolypeptides, primers, vectors, and host cells described herein can beused in one or more of the following methods: identification ofSaccharomyces cerevisiae, E. coli or Brassica napus, Glycine max, Zeamays or Oryza sativa and related organisms; mapping of genomes oforganisms related to Saccharomyces cerevisiae, E. coli, identificationand localization of Saccharomyces cerevisiae, E. coli or Brassica napus,Glycine max, Zea mays or Oryza sativa sequences of interest;evolutionary studies; determination of NUERP regions required forfunction; modulation of a NUERP activity; modulation of the metabolismof one or more cell functions; modulation of the transmembrane transportof one or more compounds; modulation of the enhancement of yield,especially of the NUE and/or biomass production; and modulation ofexpression of NUERP nucleic acids.

The NUERP nucleic acid molecules of the invention are also useful forevolutionary and polypeptide structural studies. The metabolic andtransport processes in which the molecules of the invention participateare utilized by a wide variety of prokaryotic and eukaryotic cells; bycomparing the sequences of the nucleic acid molecules of the presentinvention to those encoding similar enzymes from other organisms, theevolutionary relatedness of the organisms can be assessed. Similarly,such a comparison permits an assessment of which regions of the sequenceare conserved and which are not, which may aid in determining thoseregions of the polypeptide that are essential for the functioning of theenzyme. This type of determination is of value for polypeptideengineering studies and may give an indication of what the polypeptidecan tolerate in terms of mutagenesis without losing function.

Manipulation of the NUERP nucleic acid molecules of the invention mayresult in the production of NUERPs having functional differences fromthe wild-type NUERPs. These polypeptides may be improved in efficiencyor activity, may be present in greater numbers in the cell than isusual, or may be decreased in efficiency or activity. There are a numberof mechanisms by which the alteration of a NUERP of the invention maydirectly affect the yield, especially the NUE and/or biomass production.In the case of plants expressing NUERPs, increased transport can lead toincreased yield, especially an increased NUE and/or biomass production.By either increasing the number or the activity of transporter moleculeswhich transport and distribute nitrogen compounds or transport formsthereof, it may be possible to affect the nitrogen use efficiency.

The effect of the genetic modification in plants regarding the enhancedyield, particularly due to one or more improved yield related traits asdefined above, especially the NUE, can be assessed by growing themodified plant under less than suitable conditions and then analyzingthe growth characteristics and/or metabolism of the plant. Such analysistechniques are well known to one skilled in the art, and include dryweight, fresh weight, polypeptide synthesis, carbohydrate synthesis,lipid synthesis, evapotranspiration rates, general plant and/or cropyield, flowering, reproduction, seed setting, root growth, respirationrates, photosynthesis rates, etc. (Applications of HPLC in Biochemistryin: Laboratory Techniques in Biochemistry and Molecular Biology, Vol.17; Rehm et al., 1993 Biotechnology, Vol. 3, Chapter III: Productrecovery and purification, page 469-714, VCH: Weinheim; Belter P. A. etal., 1988, Bioseparations: downstream processing for biotechnology, JohnWiley and Sons; Kennedy J.F., and Cabral J.M.S., 1992, Recoveryprocesses for biological materials, John Wiley and Sons; Shaeiwitz J.A.and Henry J.D., 1988, Biochemical separations, in Ulmann's Encyclopediaof Industrial Chemistry, Vol. B3, Chapter 11, page 1-27, VCH: Weinheim;and Dechow F.J., 1989, Separation and purification techniques inbiotechnology, Noyes Publications).

For example, yeast expression vectors comprising the nucleic acidsdisclosed herein, or fragments thereof, can be constructed andtransformed into Saccharomyces cerevisiae using standard protocols. Theresulting transgenic cells can then be assayed for generation oralteration of their yield, particularly NUE and/or biomass production.Similarly, plant expression vectors comprising the nucleic acidsdisclosed herein, or fragments thereof, can be constructed andtransformed into an appropriate plant cell such as Arabidopsis, soy,rape, maize, cotton, rice, wheat, Medicago truncatula, etc., usingstandard protocols. The resulting transgenic cells and/or plants derivedtherefrom can then be assayed for yield increase, especially forgeneration or alteration of their NUE and/or biomass production.

The engineering of one or more genes according to table I and coding forthe NUERP of table II of the invention may also result in NUERPs havingaltered activities which indirectly and/or directly impact yield,especially the NUE of algae, plants, ciliates, fungi, or othermicroorganisms like C. glutamicum.

Additionally, the sequences disclosed herein, or fragments thereof, canbe used to generate knockout mutations in the genomes of variousorganisms, such as bacteria, mammalian cells, yeast cells, and plantcells (Girke, T., The Plant Journal 15, 39 (1998)). The resultantknockout cells can then be evaluated for their ability or capacity totolerate N-limited conditions for their growth, their response tovarious N-limited growth conditions, and the effect on the phenotypeand/or genotype of the mutation. For other methods of gene inactivation,see U.S. Pat. No. 6,004,804 and Puttaraju et al., Nature Biotechnology17, 246 (1999).

The aforementioned mutagenesis strategies for NUERPs resulting inincreased yield, especially in enhanced NUE and/or increased biomassproduction, are not meant to be limiting; variations on these strategieswill be readily apparent to one skilled in the art. Using suchstrategies, and incorporating the mechanisms disclosed herein, thenucleic acid and polypeptide molecules of the invention may be utilizedto generate algae, ciliates, plants, fungi, or other microorganisms likeC. glutamicum expressing mutated NUERP nucleic acid and polypeptidemolecules such that the yield, especially the NUE and/or biomassproduction, is improved.

The present invention also provides antibodies that specifically bind toa NUERP, or a portion thereof, as encoded by a nucleic acid describedherein. Antibodies can be made by many well-known methods (see, e.g.Harlow and Lane, “Antibodies; A Laboratory Manual”, Cold Spring HarborLaboratory, Cold Spring Harbor, N.Y., (1988)). Briefly, purified antigencan be injected into an animal in an amount and in intervals sufficientto elicit an immune response. Antibodies can either be purifieddirectly, or spleen cells can be obtained from the animal. The cells canthen fused with an immortal cell line and screened for antibodysecretion. The antibodies can be used to screen nucleic acid clonelibraries for cells secreting the antigen. Those positive clones canthen be sequenced. See, for example, Kelly et al., Bio/Technology 10,163 (1992); Bebbington et al., Bio/Technology 10, 169 (1992).

The phrases “selectively binds” and “specifically binds” with thepolypeptide refer to a binding reaction that is determinative of thepresence of the polypeptide in a heterogeneous population ofpolypeptides and other biologics. Thus, under designated immunoassayconditions, the specified antibodies bound to a particular polypeptidedo not bind in a significant amount to other polypeptides present in thesample. Selective binding of an antibody under such conditions mayrequire an antibody that is selected for its specificity for aparticular polypeptide. A variety of immunoassay formats may be used toselect antibodies that selectively bind with a particular polypeptide.For example, solid-phase ELISA immunoassays are routinely used to selectantibodies selectively immunoreactive with a polypeptide. See Harlow andLane, “Antibodies, A Laboratory Manual,” Cold Spring HarborPublications, New York, (1988), for a description of immunoassay formatsand conditions that could be used to determine selective binding. Insome instances, it is desirable to prepare monoclonal antibodies fromvarious hosts. A description of techniques for preparing such monoclonalantibodies may be found in Stites et al., eds., “Basic and ClinicalImmunology,” (Lange Medical Publications, Los Altos, Calif., FourthEdition) and references cited therein, and in Harlow and Lane,“Antibodies, A Laboratory Manual,” Cold Spring Harbor Publications, NewYork, (1988).

Gene expression in plants is regulated by the interaction of proteintranscription factors with specific nucleotide sequences within theregulatory region of a gene. One example of transcription factors arepolypeptides that contain zinc finger (ZF) motifs. Each ZF module isapproximately 30 amino acids long folded around a zinc ion. The DNArecognition domain of a ZF protein is a α-helical structure that insertsinto the major grove of the DNA double helix. The module contains threeamino acids that bind to the DNA with each amino acid contacting asingle base pair in the target DNA sequence. ZF motifs are arranged in amodular repeating fashion to form a set of fingers that recognize acontiguous DNA sequence. For example, a three-fingered ZF motif willrecognize 9 by of DNA. Hundreds of proteins have been shown to containZF motifs with between 2 and 37 ZF modules in each protein (Isalan M. etal., Biochemistry 37 (35),12026 (1998); Moore M. et al., Proc. Natl.Acad. Sci. USA 98 (4), 1432 (2001) and Moore M. et al., Proc. Natl.Acad. Sci. USA 98 (4), 1437 (2001); U.S. Pat. Nos. 6,007,988 and6,013,453).

The regulatory region of a plant gene contains many short DNA sequences(cis-acting elements) that serve as recognition domains fortranscription factors, including ZF proteins. Similar recognitiondomains in different genes allow the coordinate expression of severalgenes encoding enzymes in a metabolic pathway by common transcriptionfactors. Variation in the recognition domains among members of a genefamily facilitates differences in gene expression within the same genefamily, for example, among tissues and stages of development and inresponse to environmental conditions. Typical ZF proteins contain notonly a DNA recognition domain but also a functional domain that enablesthe ZF protein to activate or repress transcription of a specific gene.Experimentally, an activation domain has been used to activatetranscription of the target gene (U.S. Pat. No. 5,789,538 and patentapplication WO 95/19431), but it is also possible to link atranscription repressor domain to the ZF and thereby inhibittranscription (patent applications WO 00/47754 and WO 01/002019). It hasbeen reported that an enzymatic function such as nucleic acid cleavagecan be linked to the ZF (patent application WO 00/20622).

The invention provides a method that allows one skilled in the art toisolate the regulatory region of one or more NUERP encoding genes fromthe genome of a plant cell and to design zinc finger transcriptionfactors linked to a functional domain that will interact with theregulatory region of the gene. The interaction of the zinc fingerprotein with the plant gene can be designed in such a manner as to alterexpression of the gene and preferably thereby to confer increased yield,especially enhanced NUE and/or increased biomass production.

In particular, the invention provides a method of producing a transgenicplant with a NUERP coding nucleic acid, wherein expression of thenucleic acid(s) in the plant results in increased yield, especially inenhanced NUE and/or increased biomass production, as compared to a wildtype plant comprising: (a) transforming a plant cell with an expressionvector comprising a NUERP encoding nucleic acid, and (b) generating fromthe plant cell a transgenic plant with enhanced NUE and/or increasedbiomass production as compared to a wild type plant. For such planttransformation, binary vectors such as pBinAR can be used (Höfgen andWillmitzer, Plant Science 66, 221 (1990)). Moreover suitable binaryvectors are for example pBIN19, pBI101, pGPTV or pPZP (Hajukiewicz P. etal., Plant Mol. Biol., 25, 989 (1994)).

Construction of the binary vectors can be performed by ligation of thecDNA into the T-DNA. 5′ to the cDNA a plant promoter activatestranscription of the cDNA. A polyadenylation sequence is located 3′ tothe cDNA. Tissue-specific expression can be achieved by using a tissuespecific promoter as listed above. Also, any other promoter element canbe used. For constitutive expression within the whole plant, the CaMV35S promoter can be used. The expressed protein can be targeted to acellular compartment using a signal peptide, for example for plastids,mitochondria or endoplasmic reticulum (Kermode, Crit. Rev. Plant Sci. 4(15), 285 (1996)). The nucleic acid encoding the signal peptide iscloned 5′ in frame to the cDNA to archive subcellular localization ofthe fusion protein. One skilled in the art will recognize that thepromoter used should be operatively linked to the nucleic acid such thatthe promoter causes transcription of the nucleic acid which results inthe synthesis of a mRNA which encodes a polypeptide.

Alternate methods of transfection include the direct transfer of DNAinto developing flowers via electroporation or Agrobacterium mediatedgene transfer. Agrobacterium mediated plant transformation can beperformed using for example the GV3101(pMP90) (Koncz and Schell, Mol.Gen. Genet. 204, 383 (1986)) or LBA4404 (Ooms et al., Plasmid, 7, 15(1982); Hoekema et al., Nature, 303, 179 (1983)) Agrobacteriumtumefaciens strain. Transformation can be performed by standardtransformation and regeneration techniques (Deblaere et al., Nucl.Acids. Res. 13, 4777 (1994); Gelvin and Schilperoort, Plant MolecularBiology Manual, 2^(nd) Ed.—Dordrecht: Kluwer Academic Publ., 1995.—inSect., Ringbuc Zentrale Signatur: BT11-P ISBN 0-7923-2731-4; Glick B.R.and Thompson J.E., Methods in Plant Molecular Biology and Biotechnology,Boca Raton: CRC Press, 1993.-360 S., ISBN 0-8493-5164-2). For example,rapeseed can be transformed via cotyledon or hypocotyl transformation(Moloney et al., Plant Cell Reports 8, 238 (1989); De Block et al.,Plant Physiol. 91, 694 (1989)). Use of antibiotics for Agrobacterium andplant selection depends on the binary vector and the Agrobacteriumstrain used for transformation. Rapeseed selection is normally performedusing kanamycin as selectable plant marker. Agrobacterium mediated genetransfer to flax can be performed using, for example, a techniquedescribed by Mlynarova et al., Plant Cell Report 13, 282 (1994)).Additionally, transformation of soybean can be performed using forexample a technique described in European Patent No. 424 047, U.S. Pat.No. 5,322,783, European Patent No. 397 687, U.S. Pat. No. 5,376,543 orU.S. Pat. No. 5,169,770. Transformation of maize can be achieved byparticle bombardment, polyethylene glycol mediated DNA uptake or via thesilicon carbide fiber technique (see, for example, Freeling and Walbot“The maize handbook” Springer Verlag: New York (1993) ISBN3-540-97826-7). A specific example of maize transformation is found inU.S. Pat. No. 5,990,387 and a specific example of wheat transformationcan be found in PCT Application No. WO 93/07256.

Growing the modified plants under defined N-conditions, in an especialembodiment under N-limited conditions, and then screening and analyzingthe growth characteristics and/or metabolic activity assess the effectof the genetic modification in plants on enhanced NUE and/or increasedbiomass production. The same applies for the other traits of the presentinvention, too. Such analysis techniques are well known to one skilledin the art. They include beneath to screening (Römpp LexikonBiotechnologie, Stuttgart/New York: Georg Thieme Verlag 1992,“screening” p. 701) dry weight, fresh weight, protein synthesis,carbohydrate synthesis, lipid synthesis, evapotranspiration rates,general plant and/or crop yield, flowering, reproduction, seed setting,root growth, respiration rates, photosynthesis rates, etc. (Applicationsof HPLC in Biochemistry in: Laboratory Techniques in Biochemistry andMolecular Biology, Vol. 17; Rehm et al., 1993 Biotechnology, Vol. 3,Chapter III: Product recovery and purification, page 469-714, VCH:Weinheim; Belter, P. A. et al., 1988 Bioseparations: downstreamprocessing for biotechnology, John Wiley and Sons; Kennedy J.F. andCabral J.M.S., 1992 Recovery processes for biological materials, JohnWiley and Sons; Shaeiwitz J.A. and Henry J.D., 1988 Biochemicalseparations, in: Ullmann's Encyclopedia of Industrial Chemistry, Vol.B3, Chapter 11, page 1-27, VCH: Weinheim; and Dechow F.J. (1989)Separation and purification techniques in biotechnology, NoyesPublications).

In one embodiment, the present invention relates to a method for theidentification of a gene product conferring increased nutrient useefficiency and optionally enhanced tolerance to abiotic stress and/orincreased yield, in the absence of stress as well as in the absence ofnutrient deficiency, especially an enhanced NUE and/or increased biomassproduction, as compared to a corresponding non-transformed wild typecell in a cell of an organism for example plant, comprising thefollowing steps:

-   (a) contacting, e.g. hybridizing, some or all nucleic acid molecules    of a sample, e.g. cells, tissues, plants or microorganisms or a    nucleic acid library, which can contain a candidate gene encoding a    gene product conferring increased nutrient use efficiency and    optionally enhanced tolerance to abiotic stress and/or increased    yield, in the absence of stress as well as in the absence of    nutrient deficiency, especially an enhanced NUE efficiency and/or    increased biomass, with a nucleic acid molecule as shown in column 5    or 7 of table I A or B, application no. 1, or a functional homologue    thereof;-   (b) identifying the nucleic acid molecules, which hybridize under    relaxed stringent conditions with said nucleic acid molecule, in    particular to the nucleic acid molecule sequence shown in column 5    or 7 of table I, application no. 1, and, optionally, isolating the    full length cDNA clone or complete genomic clone;-   (c) identifying the candidate nucleic acid molecules or a fragment    thereof in host cells, preferably in a plant cell;-   (d) increasing the expressing of the identified nucleic acid    molecules in the host cells for which increased nutrient use    efficiency and optionally enhanced tolerance to abiotic stress    and/or and/or increased yield, in the absence of stress as well as    in the absence of nutrient deficiency, especially an enhanced NUE    and/or increased biomass production, are desired;-   (e) assaying the level of enhanced NUE and/or increased biomass    production of the host cells; and-   (f) identifying the nucleic acid molecule and its gene product which    increased expression confers increased nutrient use efficiency and    optionally enhanced tolerance to abiotic stress and/or and/or    increased yield, in the absence of stress as well as in the absence    of nutrient deficiency, especially an enhanced NUE and/or increased    biomass production, in the host cell compared to the wild type.    Relaxed hybridization conditions are: After standard hybridization    procedures washing steps can be performed at low to medium    stringency conditions usually with washing conditions of 40°-55° C.    and salt conditions between 2×SSC and 0,2×SSC with 0,1% SDS in    comparison to stringent washing conditions as e.g. 60° to 68° C.    with 0,1% SDS. Further examples can be found in the references    listed above for the stringend hybridization conditions. Usually    washing steps are repeated with increasing stringency and length    until a useful signal to noise ratio is detected and depend on many    factors as the target, e.g. its purity, GC-content, size etc, the    probe, e.g. its length, is it a RNA or a DNA probe, salt conditions,    washing or hybridization temperature, washing or hybridization time    etc.

In another embodiment, the present invention relates to a method for theidentification of a gene product the expression of which confers anincreased nutrient use efficiency and optionally enhanced tolerance toabiotic stress and/or and/or increased yield, in the absence of stressas well as in the absence of nutrient deficiency, especially an enhancedNUE and/or increased biomass production, in a cell, comprising thefollowing steps:

-   (a) identifiying a nucleic acid molecule in an organism, which is at    least 20%, preferably 25%, more preferably 30%, even more preferred    are 35%. 40% or 50%, even more preferred are 60%, 70% or 80%, most    preferred are 90% or 95% or more homolog to the nucleic acid    molecule encoding a protein comprising the polypeptide molecule as    shown in column 5 or 7 of table II, application no. 1, or comprising    a consensus sequence or a polypeptide motif as shown in column 7 of    table IV, application no. 1, or being encoded by a nucleic acid    molecule comprising a polynucleotide as shown in column 5 or 7 of    table I application no. 1, or a homologue thereof as described    herein, for example via homology search in a data bank;-   (b) enhancing the expression of the identified nucleic acid    molecules in the host cells;-   (c) assaying the level of increase of nutrient use efficiency and    optionally enhancement of tolerance to abiotic stress and/or and/or    increase of yield, in the absence of stress as well as in the    absence of nutrient deficiency, especially an enhancement of NUE    and/or increased biomass production, in the host cells; and-   (d) identifying the host cell, in which the enhanced expression    confers increased nutrient use efficiency and optionally enhanced    tolerance to abiotic stress and/or and/or increased yield, in the    absence of stress as well as in the absence of nutrient deficiency,    especially an enhanced NUE and/or increased biomass production, in    the host cell compared to a wild type.

Further, the nucleic acid molecule disclosed herein, in particular thenucleic acid molecule shown column 5 or 7 of table I A or B, applicationno. 1, may be sufficiently homologous to the sequences of relatedspecies such that these nucleic acid molecules may serve as markers forthe construction of a genomic map in related organism or for associationmapping. Furthermore natural variation in the genomic regionscorresponding to nucleic acids disclosed herein, in particular thenucleic acid molecule shown column 5 or 7 of table I A or B, applicationno. 1, or homologous thereof may lead to variation in the activity ofthe proteins disclosed herein, in particular the proteins comprisingpolypeptides as shown in column 5 or 7 of table II A or B, applicationno. 1, or comprising the consensus sequence or the polypeptide motif asshown in column 7 of table IV, application no. 1, and their homolgousand in consequence in a natural variation of increased nutrient useefficiency and optionally enhanced tolerance to abiotic stress and/orand/or increased yield, in the absence of stress as well as in theabsence of nutrient deficiency, especially of NUE and/or biomassproduction.

In consequence natural variation eventually also exists in form of moreactive allelic variants leading already to a relative increase in thetolerance to abiotic environmental stress and/or nutrient useefficiency, especially enhancement of NUE and/or biomass production,and/or yield. Different variants of the nucleic acids molecule disclosedherein, in particular the nucleic acid comprising the nucleic acidmolecule as shown column 5 or 7 of table I A or B, application no. 1,which corresponds to different enhancement of yield levels, particularlydue to one or more improved yield related traits as defined above,especially NUE and/or biomass production levels, can be indentified andused for marker assisted breeding for enhanced yield, especially NUEand/or increased biomass production.

Accordingly, the present invention relates to a method for breedingplants with enhanced yield, especially enhanced nutrient use efficiency,in particular NUE and/or increased biomass production, and optionallyenhanced abiotic stress tolerance and/or increased yield, in the absenceof stress as well as nutrient deficiencies, comprising

-   (a) selecting a first plant variety with enhanced yield, especially    enhanced nutrient use efficiency, in particular NUE and/or increased    biomass production, and optionally enhanced abiotic stress tolerance    and/or increased yield, in the absence of stress as well as nutrient    deficiencies, based on increased expression of a nucleic acid of the    invention as disclosed herein, in particular of a nucleic acid    molecule comprising a nucleic acid molecule as shown in column 5 or    7 of table I A or B, application no. 1, or a polypeptide comprising    a polypeptide as shown in column 5 or 7 of table II A or B,    application no. 1, or comprising a consensus sequence or a    polypeptide motif as shown in column 7 of table IV, application no.    1, or a homologue thereof as described herein;-   (b) associating the level of enhancement of yield, especially of the    nutrient use efficiency, in particular the NUE and/or biomass    production, and optionally enhanced abiotic stress tolerance and/or    increased yield, in the absence of stress as well as nutrient    deficiencies, with the expression level or the genomic structure of    a gene encoding said polypeptide or said nucleic acid molecule;-   (c) crossing the first plant variety with a second plant variety,    which significantly differs in its level of enhancement of yield,    especially enhanced nutrient use efficiency, in particular NUE    and/or biomass production; and-   (d) identifying, which of the offspring varieties has got increased    levels of enhanced NUE and/or biomass production by the expression    level of said polypeptide or nucleic acid molecule or the genomic    structure of the genes encoding said polypeptide or nucleic acid    molecule of the invention.    In one embodiment, the expression level of the gene according to    step (b) is increased.

Yet another embodiment of the invention relates to a process for theidentification of a compound conferring enhanced yield, especiallyenhanced nutrient use efficiency, in particular enhanced NUE and/orincreased biomass production, and optionally enhanced abiotic stresstolerance and/or increased yield, in the absence of stress as well asnutrient deficiencies, as compared to a corresponding non-transformedwild type plant cell, a plant or a part thereof in a plant cell, a plantor a part thereof, a plant or a part thereof, comprising the steps:

-   (a) culturing a plant cell; a plant or a part thereof maintaining a    plant expressing the polypeptide as shown in column 5 or 7 of table    II, application no. 1, or being encoded by a nucleic acid molecule    comprising a polynucleotide as shown in column 5 or 7 of table I,    application no. 1, or a homologue thereof as described herein or a    polynucleotide encoding said polypeptide and conferring enhanced    yield, especially enhanced nutrient use efficiency, in particular an    enhanced NUE and/or increased biomass production, and optionally    enhanced abiotic stress tolerance and/or increased yield, in the    absence of stress as well as nutrient deficiencies, as compared to a    corresponding non-transformed wild type plant cell, a plant or a    part thereof; a non-transformed wild type plant or a part thereof    and providing a readout system capable of interacting with the    polypeptide under suitable conditions which permit the interaction    of the polypeptide with this readout system in the presence of a    chemical compound or a sample comprising a plurality of chemical    compounds and capable of providing a detectable signal in response    to the binding of a chemical compound to said polypeptide under    conditions which permit the expression of said readout system and of    the protein as shown in column 5 or 7 of table II, application no.    1, or being encoded by a nucleic acid molecule comprising a    polynucleotide as shown in column 5 or 7 of table I application no.    1, or a homolog thereof as described herein; and-   (b) identifying if the chemical compound is an effective agonist by    detecting the presence or absence or decrease or increase of a    signal produced by said readout system.

Said compound may be chemically synthesized or microbiologicallyproduced and/or comprised in, for example, samples, e.g., cell extractsfrom, e.g., plants, animals or microorganisms, e.g. pathogens.Furthermore, said compound(s) may be known in the art but hitherto notknown to be capable of suppressing the polypeptide of the presentinvention. The reaction mixture may be a cell free extract or maycomprise a cell or tissue culture. Suitable set ups for the process foridentification of a compound of the invention are known to the personskilled in the art and are, for example, generally described in Albertset al., Molecular Biology of the Cell, third edition (1994), inparticular Chapter 17. The compounds may be, e.g., added to the reactionmixture, culture medium, injected into the cell or sprayed onto theplant.

If a sample containing a compound is identified in the process, then itis either possible to isolate the compound from the original sampleidentified as containing the compound capable of activating or enhancingenhanced yield, especially enhanced nutrient use efficiency, inparticular the NUE and/or increased biomass production, and optionallyenhanced abiotic stress tolerance and/or increased yield, in the absenceof stress as well as nutrient deficiencies, as compared to acorresponding non-transformed wild type, or one can further subdividethe original sample, for example, if it consists of a plurality ofdifferent compounds, so as to reduce the number of different substancesper sample and repeat the method with the subdivisions of the originalsample. Depending on the complexity of the samples, the steps describedabove can be performed several times, preferably until the sampleidentified according to the said process only comprises a limited numberof or only one substance(s). Preferably said sample comprises substancesof similar chemical and/or physical properties, and most preferably saidsubstances are identical. Preferably, the compound identified accordingto the described method above or its derivative is further formulated ina form suitable for the application in plant breeding or plant cell andtissue culture.

The compounds which can be tested and identified according to saidprocess may be expression libraries, e.g., cDNA expression libraries,peptides, proteins, nucleic acids, antibodies, small organic compounds,hormones, peptidomimetics, PNAs or the like (Milner, Nature Medicine 1,879 (1995); Hupp, Cell 83, 237 (1995); Gibbs, Cell 79, 193 (1994), andreferences cited supra). Said compounds can also be functionalderivatives or analogues of known inhibitors or activators. Methods forthe preparation of chemical derivatives and analogues are well known tothose skilled in the art and are described in, for example, Beilstein,Handbook of Organic Chemistry, Springer, New York Inc., 175 FifthAvenue, New York, N.Y. 10010 U.S.A. and Organic Synthesis, Wiley, NewYork, USA. Furthermore, said derivatives and analogues can be tested fortheir effects according to methods known in the art. Furthermore,peptidomimetics and/or computer aided design of appropriate derivativesand analogues can be used, for example, according to the methodsdescribed above. The cell or tissue that may be employed in the processpreferably is a host cell, plant cell or plant tissue of the inventiondescribed in the embodiments hereinbefore.

Thus, in a further embodiment the invention relates to a compoundobtained or identified according to the method for identifying anagonist of the invention said compound being an antagonist of thepolypeptide of the present invention.

Accordingly, in one embodiment, the present invention further relates toa compound identified by the method for identifying a compound of thepresent invention.

In one embodiment, the invention relates to an antibody specificallyrecognizing the compound or agonist of the present invention.

The invention also relates to a diagnostic composition comprising atleast one of the aforementioned nucleic acid molecules, antisensenucleic acid molecule, RNAi, snRNA, dsRNA, siRNA, miRNA, ta-siRNA,cosuppression molecule, ribozyme, vectors, proteins, antibodies orcompounds of the invention and optionally suitable means for detection.

The diagnostic composition of the present invention is suitable for theisolation of mRNA from a cell and contacting the mRNA so obtained with aprobe comprising a nucleic acid probe as described above underhybridizing conditions, detecting the presence of mRNA hybridized to theprobe, and thereby detecting the expression of the protein in the cell.Further methods of detecting the presence of a protein according to thepresent invention comprise immunotechniques well known in the art, forexample enzyme linked immunoadsorbent assay. Furthermore, it is possibleto use the nucleic acid molecules according to the invention asmolecular markers or primers in plant breeding. Suitable means fordetection are well known to a person skilled in the art, e.g. buffersand solutions for hydridization assays, e.g. the afore-mentionedsolutions and buffers, further and means for Southern-, Western-,Northern- etc. —blots, as e.g. described in Sambrook et al. are known.In one embodiment diagnostic composition contain PCR primers designed tospecifically detect the presence or the expression level of the nucleicacid molecule to be reduced in the process of the invention, e.g. of thenucleic acid molecule of the invention, or to discriminate betweendifferent variants or alleles of the nucleic acid molecule of theinvention or which activity is to be reduced in the process of theinvention.

In another embodiment, the present invention relates to a kit comprisingthe nucleic acid molecule, the vector, the host cell, the polypeptide,or the antisense, RNAi, snRNA, dsRNA, siRNA, miRNA, ta-siRNA,cosuppression molecule, or ribozyme molecule, or the viral nucleic acidmolecule, the antibody, plant cell, the plant or plant tissue, theharvestable part, the propagation material and/or the compound and/oragonist identified according to the method of the invention.

The compounds of the kit of the present invention may be packaged incontainers such as vials, optionally with/in buffers and/or solution. Ifappropriate, one or more of said components might be packaged in one andthe same container. Additionally or alternatively, one or more of saidcomponents might be adsorbed to a solid support as, e.g. anitrocellulose filter, a glas plate, a chip, or a nylon membrane or tothe well of a micro titerplate. The kit can be used for any of theherein described methods and embodiments, e.g. for the production of thehost cells, transgenic plants, pharmaceutical compositions, detection ofhomologous sequences, identification of antagonists or agonists, as foodor feed or as a supplement thereof or as supplement for the treating ofplants, etc.

Further, the kit can comprise instructions for the use of the kit forany of said embodiments.

In one embodiment said kit comprises further a nucleic acid moleculeencoding one or more of the aforementioned protein, and/or an antibody,a vector, a host cell, an anti-sense nucleic acid, a plant cell or planttissue or a plant. In another embodiment said kit comprises PCR primersto detect and discriminate the nucleic acid molecule to be reduced inthe process of the invention, e.g. of the nucleic acid molecule of theinvention.

In a further embodiment, the present invention relates to a method forthe production of an agricultural composition providing the nucleic acidmolecule for the use according to the process of the invention, thenucleic acid molecule of the invention, the vector of the invention, theantisense, RNAi, snRNA, dsRNA, siRNA, miRNA, ta-siRNA, cosuppressionmolecule, ribozyme, or antibody of the invention, the viral nucleic acidmolecule of the invention, or the polypeptide of the invention orcomprising the steps of the method according to the invention for theidentification of said compound or agonist; and formulating the nucleicacid molecule, the vector or the polypeptide of the invention or theagonist, or compound identified according to the methods or processes ofthe present invention or with use of the subject matters of the presentinvention in a form applicable as plant agricultural composition.

In another embodiment, the present invention relates to a method for theproduction of the plant culture composition comprising the steps of themethod of the present invention; and formulating the compound identifiedin a form acceptable as agricultural composition.

Under “acceptable as agricultural composition” is understood, that sucha composition is in agreement with the laws regulating the content offungicides, plant nutrients, herbicides, etc. Preferably such acomposition is without any harm for the protected plants and the animals(humans included) fed therewith.

Throughout this application, various publications are referenced. Thedisclosures of all of these publications and those references citedwithin those publications in their entireties are hereby incorporated byreference into this application in order to more fully describe thestate of the art to which this invention pertains.

It should also be understood that the foregoing relates to preferredembodiments of the present invention and that numerous changes andvariations may be made therein without departing from the scope of theinvention. The invention is further illustrated by the followingexamples, which are not to be construed in any way as limiting. On thecontrary, it is to be clearly understood that various other embodiments,modifications and equivalents thereof, which, after reading thedescription herein, may suggest themselves to those skilled in the artwithout departing from the spirit of the present invention and/or thescope of the claims.

EXAMPLE 1

Engineering Arabidopsis plants expressing genes of the presentinvention, especially with enhanced NUE and/or increased biomassproduction by over-expressing NUE related protein genes.

Cloning of the inventive sequences as shown in table I, column 5 and 7,application no. 1, for the expression in plants. Unless otherwisespecified, standard methods as described in Sambrook et al., MolecularCloning: A laboratory manual, Cold Spring Harbor 1989, Cold SpringHarbor Laboratory Press are used.

The inventive sequences as shown in table I, column 5 and 7, applicationno. 1, were amplified by PCR as described in the protocol of the PfuTurbo or Herculase DNA polymerase (Stratagene).

Sequences as shown in table I, column 5, marked with asterisk * reflectthe respective sequence derived from public data base information.

The composition for the protocol of the Pfu Turbo or Herculase DNApolymerase was as follows: 1×PCR buffer (Stratagene), 0.2 mM of eachdNTP, 100 ng genomic DNA of Saccharomyces cerevisiae (strain S288C;Research Genetics, Inc., now Invitrogen), Escherichia coli (strainMG1655; E. coli Genetic Stock Center), 50 μmol forward primer, 50 μmolreverse primer, 2.5 u Pfu Turbo or Herculase DNA polymerase.

The amplification cycles were as follows:

1 cycle of 3 minutes at 94-95° C., followed by 25-36 cycles of in eachcase 1 minute at 95° C. or 30 seconds at 94° C., 45 seconds at 50° C.,30 seconds at 50° C. or 30 seconds at 55° C. and 210-480 seconds at 72°C., followed by 1 cycle of 8 minutes at 72° C., then 4° C. —preferablyfor Saccharomyces cerevisiae; or

1 cycle of 2-3 minutes at 94° C., followed by 25-30 cycles of in eachcase 30 seconds at 94° C., 30 seconds at 55-60° C. and 5-10 minutes at72° C., followed by 1 cycle of 10 minutes at 72° C., then 4° C.—preferably for Escherichia coli.

RNA were generated with the RNeasy Plant Kit according to the standardprotocol (Qiagen) and Supersript II Reverse Transkriptase was used toproduce double stranded cDNA according to the standard protocol(Invitrogen).

The following adapter sequences were added to Saccharomyces cerevisiaeORF specific primers (see table III) for cloning purposes:

SEQ ID NO 7 i) foward primer: 5′-GGAATTCCAGCTGACCACC-3′ SEQ ID NO 8 ii)reverse primer: 5′-GATCCCCGGGAATTGCCATG-3′

The following adapter sequences were added to Escherichia coli orSynechocystis sp. ORF specific primers for cloning purposes:

SEQ ID NO 9 iii) forward primer: 5′-TTGCTCTTCC- 3′ SEQ ID NO 10 iv)reverse primer: 5′-TTGCTCTTCG-3′

Therefore for amplification and cloning of Saccharomyces cerevisiae SEQID NO: 3868, a primer consisting of the adaptor sequence i) and the ORFspecific sequence SEQ ID NO: 3878 and a second primer consisting of theadaptor sequence ii) and the ORF specific sequence SEQ ID NO: 3879 wereused.

For amplification and cloning of Echerischia coli SEQ ID NO: 38, aprimer consisting of the adaptor sequence iii) and the ORF specificsequence SEQ ID NO: 40 and a second primer consisting of the adaptorsequence iiii) and the ORF specific sequence SEQ ID NO: 41 were used.

Following these examples every sequence disclosed in table I, preferablycolumn 5, can be cloned by fusing the adaptor sequences to therespective specific primers sequences as disclosed in table III, column7.

Construction of binary vectors for non-targeted and plastid targetedexpression of proteins.

For non-targeted expression the binary vectors used for cloning wereVC-MME220-1 SEQ ID NO 1 (FIG. 1 a) and VC-MME220-1qcz SEQ ID NO 14389(FIG. 1 b) VC-MME221-1 SEQ ID NO 2 (FIG. 2 a) and VC-MME221-1qcz SEQ IDNO 14390 (FIG. 2 b), and VC-MME489-1p SEQ ID NO 15 (FIG. 5 a) andVC-MME489-1QCZ SEQ ID NO: 14395 (FIG. 5 b), respectively. The binaryvectors used for cloning the targeting sequence were VC-MME489-1p SEQ IDNO 15 (FIG. 5 a) and VC-MME489-1 QCZ SEQ ID NO: 14395 (FIG. 5 b), andpMTX0270p SEQ ID NO 16 (FIG. 6), respectively. Other useful binaryvectors are known to the skilled worker; an overview of binary vectorsand their use can be found in Hellens R., Mullineaux P. and Klee H.,(Trends in Plant Science, 5 (10), 446 (2000)). Such vectors have to beequally equipped with appropriate promoters and targeting sequences.

Amplification of the Targeting Sequence of the Gene FNR from Spinaciaoleracea

In order to amplify the targeting sequence of the FNR gene from S.oleracea, genomic DNA was extracted from leaves of 4 weeks old S.oleracea plants (DNeasy Plant Mini Kit, Qiagen, Hilden). The gDNA wasused as the template for a PCR.

To enable cloning of the transit sequence into the vector VC-MME0489-1pan EcoRI restriction enzyme recognition sequence was added to both theforward and reverse primers, whereas for cloning in the vectorspMTX0270p a PmeI restriction enzyme recognition sequence was added tothe forward primer and a NcoI site was added to the reverse primer.

FNR5EcoResgen SEQ ID NO 11 ATA GAA TTC GCA TAA ACT TAT CTT CAT AGT TGC C FNR3EcoResgen SEQ ID NO 12 ATA GAA TTC AGA GGC GAT CTG GGC CCTFNR5PmeColic SEQ ID NO 13 ATA GTT TAA ACG CAT AAA CTT ATC TTC ATA GTT GCC FNR3NcoColic SEQ ID NO 14ATA CCA TGG AAG AGC AAG AGG CGA TCT GGG CCC  T

The resulting sequence SEQ ID NO: 36 amplified from genomic spinach DNA,comprised a 5″UTR (bp 1-165), and the coding region (bp 166-273 and351-419). The coding sequence is interrupted by an intronic sequencefrom by 274 to by 350:

(SEQ ID NO 36)gcataaacttatcttcatagttgccactccaatttgctccttgaatctcctccacccaatacataatccactcctccatcacccacttcactactaaatcaaacttaactctgtttttctctctcctcctttcatttcttattcttccaatcatcgtactccgccatgaccaccgctgtcaccgccgctgtttctttcccctctaccaaaaccacctctctctccgcccgaagctcctccgtcatttcccctgacaaaatcagctacaaaaaggtgattcccaatttcactgtgttttttattaataatttgttattttgatgatgagatgattaatttgggtgctgcaggttcctttgtactacaggaatgtatctgcaactgggaaaatgggacccatcagggcccagatcgcctct

The PCR fragment derived with the primers FNR5EcoResgen andFNR3EcoResgen was digested with EcoRI and ligated in the vectorVC-MME0489-1p that had also been digested with EcoRI. The correctorientation of the FNR targeting sequence was tested by sequencing. Thevectors generated in this ligation step were VC-MME354-1 SEQ ID NO 3 andVC-MME354-1QCZ SEQ ID NO 14391.

The PCR fragment derived with the primers FNR5PmeColi and FNR3NcoColiwas digested with SmaI and NcoI and ligated in the vector pMTX0270p SEQID NO 16 (FIG. 6) that had also been digested with PmeI and NcoI. Thevectors generated in this ligation step were VC-MME432-1 SEQ ID NO 5(FIG. 4 a) and VC-MME432-1qcz SEQ ID NO 14393 (FIG. 4 b), respectively.

For cloning the ORF from S. cerevisiae, like the ORF of SEQ ID NO: 3868,the vector DNA was treated with the restriction enzyme NcoI. For cloningof ORFs from E. coli the vector DNA was treated with the restrictionenzymes PacI and NcoI following the standard protocol (MBI Fermentas).The reaction was stopped by inactivation at 70° C. for 20 minutes andpurified over QIAquick columns following the standard protocol (Qiagen).

Then the PCR-product representing the amplified ORF and the vector DNAwere treated with T4 DNA polymerase according to the standard protocol(MBI Fermentas) to produce single stranded overhangs with the parameters1 unit T4 DNA polymerase at 37° C. for 2-10 minutes for the vector and 1u T4 DNA polymerase at 15° C. for 10-60 minutes for the PCR productrepresenting, like that of SEQ ID NO: 3868.

The reaction was stopped by addition of high-salt buffer and purifiedover QIAquick columns following the standard protocol (Qiagen).

According to this example the skilled person is able to clone allsequences disclosed in table I, preferably column 5.

Approximately 30 ng of prepared vector and a defined amount of preparedamplificate were mixed and hybridized at 65° C. for 15 minutes followedby 37° C. 0,1° C./1 seconds, followed by 37° C. 10 minutes, followed by0,1° C./1 seconds, then 4° C.

The ligated constructs were transformed in the same reaction vessel byaddition of competent E. coli cells (strain DHSalpha) and incubation for20 minutes at 1° C. followed by a heat shock for 90 seconds at 42° C.and cooling to 4° C. Then, complete medium (SOC) was added and themixture was incubated for 45 minutes at 37° C. The entire mixture wassubsequently plated onto an agar plate with 0.05 mg/ml kanamycine andincubated overnight at 37° C.

The outcome of the cloning step was verified by amplification with theaid of primers which bind upstream and downstream of the integrationsite, thus allowing the amplification of the insertion. Theamplifications were carried as described in the protocol of Taq DNApolymerase (Gibco-BRL).

The amplification cycles were as follows:

1 cycle of 5 minutes at 94° C., followed by 35 cycles of in each case 15seconds at 94° C., 15 seconds at 50-66° C. and 5 minutes at 72° C.,followed by 1 cycle of 10 minutes at 72° C., then 4° C.

Several colonies were checked, but only one colony for which a PCRproduct of the expected size was detected was used in the followingsteps.

A portion of this positive colony was transferred into a reaction vesselfilled with complete medium (LB) supplemented with kanamycin andincubated overnight at 37° C.

The plasmid preparation was carried out as specified in the Qiaprepstandard protocol (Qiagen).

Generation of transgenic plants which express SEQ ID NO: 3868 or anyother sequence disclosed in table I, preferably column 5

1-5 ng of the plasmid DNA isolated was transformed by electroporationinto competent cells of Agrobacterium tumefaciens, of strain GV 3101pMP90 (Koncz and Schell, Mol. Gen. Gent. 204, 383 (1986)). Thereafter,complete medium (YEP) was added and the mixture was transferred into afresh reaction vessel for 3 hours at 28° C. Thereafter, all of thereaction mixture was plated onto YEP agar plates supplemented with therespective antibiotics, e.g. rifampicine (0.1 mg/ml), gentamycine (0.025mg/ml and kanamycine (0.05 mg/ml) and incubated for 48 hours at 28° C.

The agrobacteria that contains the plasmid construct were then used forthe transformation of plants.

A colony was picked from the agar plate with the aid of a pipette tipand taken up in 3 ml of liquid TB medium, which also contained suitableantibiotics as described above. The preculture was grown for 48 hours at28° C. and 120 rpm. 400 ml of LB medium containing the same antibioticsas above were used for the main culture. The preculture was transferredinto the main culture. It was grown for 18 hours at 28° C. and 120 rpm.After centrifugation at 4 000 rpm, the pellet was resuspended ininfiltration medium (MS medium, 10% sucrose).

In order to grow the plants for the transformation, dishes (Piki Saat80, green, provided with a screen bottom, 30×20×4.5 cm, fromWiesauplast, Kunststofftechnik, Germany) were half-filled with a GS 90substrate (standard soil, Werkverband E.V., Germany). The dishes werewatered overnight with 0.05% Proplant solution (Chimac-Apriphar,Belgium). Arabidopsis thaliana C24 seeds (Nottingham Arabidopsis StockCentre, UK; NASC Stock N906) were scattered over the dish, approximately1 000 seeds per dish. The dishes were covered with a hood and placed inthe stratification facility (8 h, 110 μmol/m²s, 22° C.; 16 h, dark, 6°C.). After 5 days, the dishes were placed into the short-day controlledenvironment chamber (8 h, 130 μmol/m²s, 22° C.; 16 h, dark, 20° C.),where they remained for approximately 10 days until the first trueleaves had formed.

The seedlings were transferred into pots containing the same substrate(Teku pots, 7 cm, LC series, manufactured by Poppelmann GmbH & Co,Germany). Five plants were pricked out into each pot. The pots were thenreturned into the short-day controlled environment chamber for the plantto continue growing.

After 10 days, the plants were transferred into the greenhouse cabinet(supplementary illumination, 16 h, 340 μE/m²s, 22° C.; 8 h, dark, 20°C.), where they were allowed to grow for further 17 days.

For the transformation, 6-week-old Arabidopsis plants, which had juststarted flowering were immersed for 10 seconds into the above-describedagrobacterial suspension which had previously been treated with 10 μlSilwett L77 (Crompton S.A., Osi Specialties, Switzerland). The method inquestion is described by Clough J.C. and Bent A.F. (Plant J. 16, 735(1998)).

The plants were subsequently placed for 18 hours into a humid chamber.Thereafter, the pots were returned to the greenhouse for the plants tocontinue growing. The plants remained in the greenhouse for another 10weeks until the seeds were ready for harvesting.

Depending on the resistance marker used for the selection of thetransformed plants the harvested seeds were planted in the greenhouseand subjected to a spray selection or else first sterilized and thengrown on agar plates supplemented with the respective selection agent.Since the vector contained the bar gene as the resistance marker,plantlets were sprayed four times at an interval of 2 to 3 days with0.02% BASTA® and transformed plants were allowed to set seeds.

The seeds of the transgenic A. thaliana plants were stored in thefreezer (at −20° C.).

Plant Screening (Arabidopsis) for growth under low temperatureconditions or growth under limited nitrogen supply or growth underconditions in the absence of stress as well as nutrient deficiencies

Plant screening (Arabidopsis) for growth under limited nitrogen supply

For screening of transgenic plants a specific culture facility was used.For high-throughput purposes plants were screened for biomass productionon agar plates with limited supply of nitrogen (adapted from Estelle andSomerville, 1987). This screening pipeline consists of two levels.Transgenic lines are subjected to subsequent level if biomass productionwas significantly improved in comparison to wild type plants. With eachlevel number of replicates and statistical stringency was increased.

For the sowing, the seeds, which had been stored in the refrigerator (at−20° C.), were removed from the Eppendorf tubes with the aid of atoothpick and transferred onto the above-mentioned agar plates, withlimited supply of nitrogen (0.05 mM KNO₃). In total, approximately 15-30seeds were distributed horizontally on each plate (12×12 cm).

After the seeds had been sown, plates are subjected to stratificationfor 2-4 days in the dark at 4° C. After the stratification, the testplants were grown for 22 to 25 days at a 16-h-light, 8-h-dark rhythm at20° C., an atmospheric humidity of 60% and a CO₂ concentration ofapproximately 400 ppm. The light sources used generate a lightresembling the solar color spectrum with a light intensity ofapproximately 100 μE/m²s. After 10 to 11 days the plants areindividualized. Improved growth under nitrogen limited conditions wasassessed by biomass production of shoots and roots of transgenic plantsin comparison to wild type control plants after 20-25 days growth.

Transgenic lines showing a significant improved biomass production incomparison to wild type plants are subjected to following experiment ofthe subsequent level:

Arabidopsis thaliana seeds are sown in pots containing a 1:1 (v:v)mixture of nutrient depleted soil (“Einheitserde Typ 0”, 30% clay,Tantau, Wansdorf Germany) and sand. Germination is induced by a four dayperiod at 4° C., in the dark. Subsequently the plants are grown understandard growth conditions (photoperiod of 16 h light and 8 h dark, 20°C., 60% relative humidity, and a photon flux density of 200 μE/m²s). Theplants are grown and cultured, inter alia they are watered every secondday with a N-depleted nutrient solution. The N-depleted nutrientsolution e.g. contains beneath water

mineral nutrient final concentration KCl 3.00 mM MgSO₄ × 7 H₂O 0.5 mMCaCl₂ × 6 H₂O 1.5 mM K₂SO₄ 1.5 mM NaH₂PO₄ 1.5 mM Fe-EDTA 40 μM H₃BO₃ 25μM MnSO₄ × H₂O 1 μM ZnSO₄ × 7 H₂O 0.5 μM Cu₂SO₄ × 5 H₂O 0.3 μM Na₂MoO₄ ×2 H₂O 0.05 μM

After 9 to 10 days the plants are individualized. After a total time of29 to 31 days the plants are harvested and rated by the fresh weight ofthe aerial parts of the plants. The results thereof are summarized intable VII-A. The biomass increase has been measured as ratio of thefresh weight of the aerial parts of the respective transgene plant andthe non-transgenic wild type plant.

TABLE VII-A SeqID Target Locus Biomass Increase  38 Cytoplasmic B00171.19  42 Cytoplasmic B0045 1.15  123 Plastidic B0180 1.41  380 PlastidicB0242 1.16  679 Plastidic B0403 1.10  812 Cytoplasmic B0474 1.24 1055Plastidic B0754 1.15 1563 Cytoplasmic B0784 1.20 1705 Plastidic B08731.17 1844 Cytoplasmic B1014 1.19 1950 Plastidic B1020 1.10 1975Cytoplasmic B1180 1.23 2127 Plastidic B1933 1.55 2135 Plastidic B20321.24 2171 Plastidic B2165 1.24 2297 Plastidic B2223 1.36 2426 PlastidicB2238 1.26 2452 Plastidic B2310 1.18 2551 Plastidic B2431 1.47 2600Plastidic B2600 1.12 2668 Plastidic B2766 1.10 2772 Cytoplasmic B29031.65 3117 Plastidic B3117 1.42 3390 Plastidic B3120 1.28 3396 PlastidicB3216 1.19 3470 Plastidic B3451 1.21 3563 Cytoplasmic B3791 1.25  3770*Plastidic B3825 1.42 3868 Cytoplasmic Yal019w 1.42 3895 CytoplasmicYar035w 1.38 3953 Cytoplasmic Ybl021c 1.15 4111 Cytoplasmic Ybr055c 1.104149 Cytoplasmic YBR128C 1.19 4162 Cytoplasmic Ybr159w 1.23 4235Cytoplasmic Ybr243c 1.16 4280 Cytoplasmic Ybr262c 1.31 4288 CytoplasmicYcr019w 1.31 4315 Cytoplasmic Ydr070c 1.20 4325 Cytoplasmic Ydr079w 1.294335 Cytoplasmic Ydr123c 1.19 4346 Cytoplasmic Ydr137w 1.22 4361Cytoplasmic Ydr294c 1.13 4402 Cytoplasmic Ydr330w 1.38 4431 CytoplasmicYdr355c 1.34 4435 Plastidic YDR430C 1.16 4485 Cytoplasmic Ydr472w 1.204506 Plastidic YDR497C 1.16 4790 Cytoplasmic Yer029c 1.23 4806Cytoplasmic YFR007W 1.36 4836 Cytoplasmic YGL039W 1.22 5311 CytoplasmicYgl043w 1.26 5346 Cytoplasmic Ygr088w 1.13 5533 Cytoplasmic Ygr122c-a1.30 5551 Cytoplasmic Ygr142w 1.21 5559 Cytoplasmic Ygr143w 1.19 5602Cytoplasmic Ygr165w 1.23 5608 Cytoplasmic Ygr170w 1.12 5614 CytoplasmicYgr202c 1.55 5666 Cytoplasmic Ygr266w 1.34 5701 Cytoplasmic Ygr282c 1.215750 Cytoplasmic Ygr290w 1.19 5754 Cytoplasmic Yhl021c 1.19 5778Cytoplasmic Yhl031c 1.21 5812 Cytoplasmic Yhr011w 1.21 5967 CytoplasmicYhr127w 1.36 5973 Cytoplasmic Yhr137w 1.39 6027 Cytoplasmic Yil099w 3.096107 Cytoplasmic Yil147c 1.21  6150* Cytoplasmic Yir034c 2.42 6198Cytoplasmic Yjl013c 1.42 6208 Cytoplasmic Yjl041w 1.41 6242 CytoplasmicYjl064w 1.30 6246 Cytoplasmic Yjl067w 1.29 6250 Cytoplasmic Yjl094c 1.236297 Cytoplasmic Yjl171c 1.19 6326 Cytoplasmic Yjl213w 1.62 6488Cytoplasmic Yjr017c 1.50 6550 Cytoplasmic Yjr058c 1.28 6700 CytoplasmicYjr117w 1.81 6816 Cytoplasmic Yjr121w 1.52  7366* Cytoplasmic Yjr131w1.52 7475 Cytoplasmic Yjr145c 1.41 7602 Cytoplasmic Ykl084w 1.20 7651Cytoplasmic Ykl088w 1.23  7661* Cytoplasmic Ykl100c 1.25 7675Cytoplasmic Ykl131w 1.22 7679 Cytoplasmic Ykl138c 1.24 7710 CytoplasmicYkl178c 2.69 7735 Cytoplasmic Ykl179c 1.58  7778* Cytoplasmic Ykl193c1.77 7829 Cytoplasmic Ykl216w 2.09 8017 Cytoplasmic Ykr016w 2.00 8045Cytoplasmic Ykr021w 2.14 8073 Cytoplasmic Ykr055w 1.57 8263 PlastidicYkr088c 1.29 8287 Cytoplasmic Ykr093w 3.98 8468 Cytoplasmic Ykr099w 1.15 8484* Cytoplasmic Ykr100c 4.43 8492 Cytoplasmic Yll014w 1.61  8514*Cytoplasmic Yll016w 1.24 8539 Cytoplasmic Yll023c 1.17 8571 CytoplasmicYll037w 1.32 8575 Cytoplasmic Yll049w 1.75 8579 Cytoplasmic Yll055w 5.25 8661* Cytoplasmic Ylr034c 4.38 8991 Cytoplasmic Ylr042c 1.40 8995Cytoplasmic Ylr053c 1.55 8999 Cytoplasmic Ylr058c 1.19  9551*Cytoplasmic Ylr060w 3.72 9637 Cytoplasmic Ylr065c 1.88 9672 CytoplasmicYlr070c 2.66 10182  Cytoplasmic Ylr00w 1.57 10214  Cytoplasmic Ylr109w1.55 10447  Cytoplasmic Ylr125w 1.28 10451  Cytoplasmic Ylr127c 1.2210463  Cytoplasmic Ylr185w 1.14 10533  Cytoplasmic Ylr204w 1.38 10541 Cytoplasmic Ylr242c 1.61 10562  Cytoplasmic Ylr293c 2.75 10990 Cytoplasmic Ylr313c 1.25 10998  Cytoplasmic Ylr315w 1.54 11004 Cytoplasmic Ylr329w 1.27 11012  Cytoplasmic Ylr362w 3.40 11054 Cytoplasmic Ylr395c 1.56 11066  Cytoplasmic Ylr404w 1.33 11074 Cytoplasmic Ylr463c 1.33 11080  Cytoplasmic Yml022w 1.27 11552 Cytoplasmic Yml027w 1.42 11569  Cytoplasmic Yml065w 1.14 11596 Cytoplasmic Yml089c 1.17 11600  Cytoplasmic Yml128c 1.12 11612 Cytoplasmic Ymr011w 1.52 12246  Cytoplasmic Ymr037c 1.41 12263 Cytoplasmic Ymr049c 3.71 12316  Cytoplasmic Ymr052w 1.28 12327*Cytoplasmic Ymr082c 1.26 12331  Cytoplasmic YMR125W 1.24 12378 Cytoplasmic Ymr126c 1.19 12394  Cytoplasmic Ymr144w 1.36 12406 Cytoplasmic Ymr160w 1.29 12414* Cytoplasmic Ymr191w 1.51 12420 Cytoplasmic Ymr209c 1.18 12440  Cytoplasmic Ymr233w 1.61 12470 Cytoplasmic Ymr278w 1.20 12749  Cytoplasmic Ymr280c 1.31 12773 Cytoplasmic Ynl014w 1.21 12829  Cytoplasmic Ynl320w 1.46 12883 Cytoplasmic Yol007c 1.15 12889  Cytoplasmic Yol164w 1.21 13014 Cytoplasmic Yor076c 1.10 13018  Cytoplasmic Yor083w 1.48 13024 Cytoplasmic Yor097c 1.19 13030  Cytoplasmic Yor128c 1.46 14085 Cytoplasmic Yor353c 1.26 14093  Cytoplasmic Ypl141c 1.33 14113 Cytoplasmic Ypr088c 1.61 14246  Cytoplasmic Ypr108w 1.25 14311 Cytoplasmic Ypr110c 1.22 14914  Plastidic B3825_2 1.42 15382 Cytoplasmic Yir034c_2 2.42 15460  Cytoplasmic Yjr131w_2 1.52 15571 Cytoplasmic Ykl100c_2 1.25 15593  Cytoplasmic Ykl193c_2 1.77 15646 Cytoplasmic Yll016w_2 1.24 15673  Cytoplasmic Ylr034c_2 4.38 16005 Cytoplasmic Ylr060w_2 3.72 16114  Cytoplasmic YMR082C_2 1.26 14402 Cytoplasmic B1258 1.36 16093  Cytoplasmic YML101C 1.35 16106 Cytoplasmic YMR065W 1.28 16120  Cytoplasmic YMR163C 1.21 16275 Cytoplasmic YOL042W 1.16 16305  Cytoplasmic YOR226C 1.24 16573 Cytoplasmic YPL068C 1.11 14396  Plastidic B0165 1.14 16299  CytoplasmicYOR203W 1.21 16133  Cytoplasmic YNL147W 1.15 15056  Cytoplasmic YBR083W1.11 15587  Cytoplasmic YKL111C 1.11 16582  Cytoplasmic YPR067W 1.1314839  Cytoplasmic B1985 1.16 15014  Cytoplasmic B3838 1.42 15432 Cytoplasmic YJL010C 1.11 14497  Cytoplasmic B1267 1.23 14718 Cytoplasmic B1322 1.33 14791  Cytoplasmic B1381 1.11 14879  CytoplasmicB2646 1.31 15064  Cytoplasmic YBR191W 1.12 15257  Cytoplasmic YDL135C1.33 15378  Cytoplasmic YHL005C 1.25 16629  Cytoplasmic YKR100C_2 4.4316647  Cytoplasmic Ymr191w_2 1.51 Sequences marked with asterisk *reflect the respective sequence derived from public data basesinformation.

Plant Screening (Arabidopsis) for Growth Under Low TemperatureConditions

In a standard experiment soil was prepared as 3.5:1 (v:v) mixture ofnutrient rich soil (GS90, Tantau, Wansdorf, Germany) and sand. Pots werefilled with soil mixture and placed into trays. Water was added to thetrays to let the soil mixture take up appropriate amount of water forthe sowing procedure. The seeds for transgenic Arabidopsis thalianaplants (created as described above) were sown in pots (6 cm diameter).Pots were collected until they filled a tray for the growth chamber.Then the filled tray was covered with a transparent lid and transferredinto the shelf system of the precooled (4° C.-5° C.) growth chamber.Stratification was established for a period of 2-3 days in the dark at4° C.-5° C. Germination of seeds and growth was initiated at a growthcondition of 20° C., 60% relative humidity, 16 h photoperiod andillumination with fluorescent light at 200 μmol/m²s. Covers were removed7 days after sowing. BASTA selection was done at day 9 after sowing byspraying pots with plantlets from the top. Therefore, a 0.07% (v:v)solution of BASTA concentrate (183 g/L glufosinate-ammonium) in tapwater was sprayed. Transgenic events and wildtype control plants weredistributed randomly over the chamber. The location of the trays insidethe chambers was changed on working days from day 7 after sowing.Watering was carried out every two days after covers were removed fromthe trays. Plants were individualized 12-13 days after sowing byremoving the surplus of seedlings leaving one seedling in a pot. Cold(chilling to 11° C.-12° C.) was applied 14 days after sowing until theend of the experiment. For measuring biomass performance, plant freshweight was determined at harvest time (29-31 days after sowing) bycutting shoots and weighing them. Besides weighing, phenotypicinformation was added in case of plants that differ from the wild typecontrol. Plants were in the stage prior to flowering and prior to growthof inflorescence when harvested.

Three successive experiments were conducted. In the first experiment,one individual of each transformed line was tested.

In the second experiment, the event that had been determined as chillingtolerant or resistant in the first experiment, i.e. showed increasedyield, in this case increased biomass production, in comparison to wildtype, were put through a confirmation screen according to the sameexperimental procedures. In this experiment, max. 10 plants of eachtolerant or resistant event were grown, treated and measured as before.

In the first two experiments, chilling tolerance or tolerance andbiomass production was compared to wild type plants.

In the third experiment, up to 20 replicates of each confirmed tolerantevent, i.e. those that had been scored as tolerant or resistant in thesecond experiment, were grown, treated and scored as before. The resultsthereof are summarized in table VII-B.

TABLE VII-B SeqID Target Locus Biomass Increase 1055 Plastidic B07541.09 1950 Plastidic B1020 1.17 2127 Plastidic B1933 1.12 2426 PlastidicB2238 1.19 2452 Plastidic B2310 1.25 2551 Plastidic B2431 1.34 2668Plastidic B2766 1.26 3117 Plastidic B3117 1.16 3390 Plastidic B3120 1.153470 Plastidic B3451 1.10 4162 Cytoplasmic Ybr159w 1.07 4235 PlastidicYbr243c 1.26 4288 Cytoplasmic Ycr019w 1.24 4325 Cytoplasmic Ydr079w 1.094346 Cytoplasmic Ydr137w 1.14 4402 Cytoplasmic Ydr330w 1.24 4435Plastidic YDR430C 1.10 4506 Plastidic YDR497C 1.23/1.24 (promoter 1/2)4790 Cytoplasmic Yer029c 1.13 4836 Cytoplasmic YGL039W 1.32 5754Cytoplasmic Yhl021c 1.12 5973 Plastidic Yhr137w 1.13 6027 PlastidicYil099w 1.20 6326 Cytoplasmic Yjl213w 1.12 7602 Cytoplasmic Ykl084w 1.107735 Cytoplasmic Ykl179c 1.22 8073 Cytoplasmic Ykr055w 1.09 8263Plastidic Ykr088c 1.20 8484 Cytoplasmic Ykr100c 1.12 10533 PlastidicYlr204w 1.22 12773 Cytoplasmic Ynl014w 1.11 14113 Cytoplasmic Ypr088c1.26 14396 Plastidic B0165 1.08 14718 Cytoplasmic B1322 1.06 14879Cytoplasmic B2646 1.11 16629 Cytoplasmic YKR100C_2 1.12

Plant Screening (Arabidopsis) for Growth Under Cycling DroughtConditions

In the cycling drought assay repetitive stress is applied to plantswithout leading to desiccation. In a standard experiment soil isprepared as 1:1 (v:v) mixture of nutrient rich soil (GS90, Tantau,Wansdorf, Germany) and quarz sand. Pots (6 cm diameter) were filled withthis mixture and placed into trays. Water was added to the trays to letthe soil mixture take up appropriate amount of water for the sowingprocedure (day 1) and subsequently seeds of transgenic A. thalianaplants and their wild-type controls were sown in pots. Then the filledtray was covered with a transparent lid and transferred into a precooled(4° C.-5° C.) and darkened growth chamber. Stratification wasestablished for a period of 3 days in the dark at 4° C.-5° C. or,alternatively, for 4 days in the dark at 4° C. Germination of seeds andgrowth was initiated at a growth condition of 20° C., 60% relativehumidity, 16 h photoperiod and illumination with fluorescent light atapproximately 200 μmol/m²s. Covers were removed 7-8 days after sowing.BASTA selection was done at day 10 or day 11 (9 or 10 days after sowing)by spraying pots with plantlets from the top. In the standardexperiment, a 0.07% (v/v) solution of BASTA concentrate (183 g/Lglufosinate-ammonium) in tap water was sprayed once or, alternatively, a0.02% (v:v) solution of BASTA was sprayed three times. The wild-typecontrol plants were sprayed with tap water only (instead of sprayingwith BASTA dissolved in tap water) but were otherwise treatedidentically. Plants were individualized 13-14 days after sowing byremoving the surplus of seedlings and leaving one seedling in soil.Transgenic events and wild-type control plants were evenly distributedover the chamber.

The water supply throughout the experiment was limited and plants weresubjected to cycles of drought and re-watering. Watering was carried outat day 1 (before sowing), day 14 or day 15, day 21 or day 22, and,finally, day 27 or day 28. For measuring biomass production, plant freshweight was determined one day after the final watering (day 28 or day29) by cutting shoots and weighing them. Besides weighing, phenotypicinformation was added in case of plants that differ from the wild typecontrol. Plants were in the stage prior to flowering and prior to growthof inflorescence when harvested.

Up to five lines (events) per transgenic construct were tested insuccessive experimental levels (up to 4). Only constructs that displayedpositive performance were subjected to the next experimental level.Usually in the first level five plants per construct were tested and inthe subsequent levels 30-60 plants were tested. Biomass performance wasevaluated as described above. Data are shown for constructs thatdisplayed increased biomass performance in at least two successiveexperimental levels in Table VII-C.

Biomass production was measured by weighing plant rosettes. Biomassincrease was calculated as ratio of average weight for transgenic plantscompared to average weight of wild type control plants from the sameexperiment. The mean biomass increase of transgenic constructs is given.

TABLE VII-C SeqID Target Locus Biomass Increase 2426 Cytoplasmic B22381.11 4361 Plastidic Ydr294c 1.35 4506 Plastidic YDR497C 1.10 9637Cytoplasmic Ylr065c 1.24

Plant Screening (Arabidopsis) for Yield Increase Under StandardizedConditions

In this experiment, a plant screening for yield increase (in this case:biomass yield increase) under standardized growth conditions in theabsence of substantial abiotic stress and biotic stress has beenperformed. In a standard experiment soil is prepared as 3.5:1 (v:v)mixture of nutrient rich soil (GS90, Tantau, Wansdorf, Germany) andquartz sand. Alternatively, plants were sown on nutrient rich soil(GS90, Tantau, Germany). Pots were filled with soil mixture and placedinto trays. Water was added to the trays to let the soil mixture take upappropriate amount of water for the sowing procedure. The seeds fortransgenic A. thaliana plants and their non-transgenic wild-typecontrols were sown in pots (6 cm diameter). Then the filled tray wascovered with a transparent lid and transferred into a precooled (4°C.-5° C.) and darkened growth chamber. Stratification was establishedfor a period of 3-4 days in the dark at 4° C.-5° C. Germination of seedsand growth was initiated at a growth condition of 20° C., 60% relativehumidity, 16 h photoperiod and illumination with fluorescent light atapproximately 200 μmol/m²s. Covers were removed 7-8 days after sowing.BASTA selection was done at day 10 or day 11 (9 or 10 days after sowing)by spraying pots with plantlets from the top. In the standardexperiment, a 0.07% (v:v) solution of BASTA concentrate (183 g/Lglufosinate-ammonium) in tap water was sprayed once or, alternatively, a0.02% (v:v) solution of BASTA was sprayed three times. The wild-typecontrol plants were sprayed with tap water only (instead of sprayingwith BASTA dissolved in tap water) but were otherwise treatedidentically. Plants were individualized 13-14 days after sowing byremoving the surplus of seedlings and leaving one seedling in soil.Transgenic events and wild-type control plants were evenly distributedover the chamber. Watering was carried out as needed, every two daysafter removing the covers in a standard experiment or, alternatively,every day. For measuring biomass performance, plant fresh weight wasdetermined at harvest time (24-29 days after sowing) by cutting shootsand weighing them. Plants were in the stage prior to flowering and priorto growth of inflorescence when harvested. Transgenic plants werecompared to the non-transgenic wild-type control plants.

Per transgenic construct up to five events, with up to 60 plants perevent, were tested in up to four experimental levels. Biomassperformance was evaluated as described below; the respective data aresummarized in table VII-D.

Biomass production was measured by harvesting and weighing plantrosettes. Biomass increase was calculated as ratio of average weight oftransgenic plants compared to average weight of wild-type control plantsfrom the same experiment. The mean biomass increase of transgenicconstructs is given.

TABLE VII-D SeqID Target Locus Biomass Increase 123 Plastidic B0180 1.33812 Cytoplasmic B0474 1.09 1055 Plastidic B0754 1.23 1975 CytoplasmicB1180 1.18 2135 Plastidic B2032 1.14 2171 Plastidic B2165 1.24 2426Plastidic B2238 1.18 2452 Plastidic B2310 1.20 2551 Plastidic B2431 1.172600 Plastidic B2600 1.16 2668 Plastidic B2766 1.20 3390 Plastidic B31201.39 3470 Plastidic B3451 1.23 3868 Cytoplasmic Yal019w 1.14 3895Cytoplasmic Yar035w 1.43 4235 Plastidic Ybr243c 1.29 4315 CytoplasmicYdr070c 1.47 4402 Cytoplasmic Ydr330w 1.14 4435 Plastidic YDR430C 1.614506 Plastidic YDR497C 1.14 4790 Cytoplasmic Yer029c 1.10 6550Cytoplasmic Yjr058c 1.36 6700 Cytoplasmic Yjr117w 1.22 6816 CytoplasmicYjr121w 1.37 7710 Cytoplasmic Ykl178c 1.57 8468 Cytoplasmic Ykr099w 1.508484 Cytoplasmic Ykr100c 1.30 8995 Cytoplasmic Ylr053c 1.17 14396Plastidic B0165 1.79 15432 Cytoplasmic YJL010C 1.47 14718 CytoplasmicB1322 1.20 14879 Cytoplasmic B2646 1.23 16629 Cytoplasmic YKR100C_2 1.30

EXAMPLE 2

Engineering Arabidopsis plants with increased yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction, and/or increased biomass production by over-expressing NUE(NUERP) related protein encoding genes from Saccharomyces cereviesae orE. coli using tissue-specific promoters and/or stress induciblepromoters.

Transgenic Arabidopsis plants are created as in example 1 to express theNUE related protein (NUERP) encoding transgenes under the control of atissue-specific promoter and/or stress inducible promoters.

T2 generation plants are produced and are grown under the respectiveconditions (low temperature, drought conditions, N-limited conditions,conditions in the absence of stress as well as nutrient deficiencies.Biomass production is determined after a total time of 29 to 31 daysstarting with the sowing. The transgenic Arabidopsis produces morebiomass than non-transgenic control plants.

EXAMPLE 3

Engineering alfalfa plants with increased yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction, by over-expressing NUE related protein (NUERP) encodinggenes from Saccharomyces cerevisiae or E. coli by over-expressing NUErelated protein (NUERP) encoding genes for example from Brassica napus,Glycine max, Zea mays or Oryza sativa for example

A regenerating clone of alfalfa (Medicago sativa) is transformed usingthe method of (McKersie et al., Plant Physiol 119, 839 (1999)).Regeneration and transformation of alfalfa is genotype dependent andtherefore a regenerating plant is required. Methods to obtainregenerating plants have been described. For example, these can beselected from the cultivar Rangelander (Agriculture Canada) or any othercommercial alfalfa variety as described by Brown D.C.W. and Atanassov A.(Plant Cell Tissue Organ Culture 4, 111 (1985)). Alternatively, the RA3variety (University of Wisconsin) is selected for use in tissue culture(Walker et al., Am. J. Bot. 65, 654 (1978)).

Petiole explants are cocultivated with an overnight culture ofAgrobacterium tumefaciens C58C1 pMP90 (McKersie et al., Plant Physiol119, 839 (1999)) or LBA4404 containing a binary vector. Many differentbinary vector systems have been described for plant transformation (e.g.An G., in Agrobacterium Protocols, Methods in Molecular Biology, Vol 44,pp 47-62, Gartland K.M.A. and Davey M.R. eds. Humana Press, Totowa,N.J.). Many are based on the vector pBIN19 described by Bevan (NucleicAcid Research. 12, 8711 (1984)) that includes a plant gene expressioncassette flanked by the left and right border sequences from the Tiplasmid of Agrobacterium tumefaciens. A plant gene expression cassetteconsists of at least two genes—a selection marker gene and a plantpromoter regulating the transcription of the cDNA or genomic DNA of thetrait gene. Various selection marker genes can be used including theArabidopsis gene encoding a mutated acetohydroxy acid synthase (AHAS)enzyme (U.S. Pat. Nos. 5,7673,666 and 6,225,105). Similarly, variouspromoters can be used to regulate the trait gene that providesconstitutive, developmental, tissue or environmental regulation of genetranscription. In this example, the 34S promoter (GenBank Accessionnumbers M59930 and X16673) is used to provide constitutive expression ofthe trait gene.

The explants are cocultivated for 3 days in the dark on SH inductionmedium containing 288 mg/L Pro, 53 mg/L thioproline, 4.35 g/L K₂SO₄, and100 μm acetosyringinone. The explants are washed in half-strengthMurashige-Skoog medium (Murashige and Skoog, 1962) and plated on thesame SH induction medium without acetosyringinone but with a suitableselection agent and suitable antibiotic to inhibit Agrobacterium growth.After several weeks, somatic embryos are transferred to BOi2Ydevelopment medium containing no growth regulators, no antibiotics, and50 g/L sucrose. Somatic embryos are subsequently germinated onhalf-strength Murashige-Skoog medium. Rooted seedlings are transplantedinto pots and grown in a greenhouse.

The T0 transgenic plants are propagated by node cuttings and rooted inTurface growth medium. T1 or T2 generation plants are produced and aregrown under the respective conditions (low temperature, droughtconditions, N-limited conditions, conditions in the absence of stress aswell as nutrient deficiencies, especially subjected to experiments withlimited nitrogen supply: Plants receive limited nitrogen supply by useof a nutrient depleted soil. Nutrients apart from nitrogen are suppliedby a nutrient solution. For NUE assessment biomass production and/or drymatter production and/or seed yield is compared to non-transgenic wildtype plants. For the other traits the procedure is adapted accordingly.

EXAMPLE 4

Engineering ryegrass plants with increased yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE, by over-expressing NUE relatedprotein (NUERP) encoding genes from Saccharomyces cerevisiae or E. colior by over-expressing NUE related protein (NUERP) encoding genes fromfor example Brassica napus, Glycine max, Zea mays or Oryza sativa.

Seeds of several different ryegrass varieties may be used as explantsources for transformation, including the commercial variety Gunneavailable from Svalof Weibull seed company or the variety Affinity.Seeds are surface-sterilized sequentially with 1% Tween-20 for 1 minute,100% bleach for 60 minutes, 3 rinses with 5 minutes each with deionizedand distilled H₂O, and then germinated for 3-4 days on moist, sterilefilter paper in the dark. Seedlings are further sterilized for 1 minutewith 1% Tween-20, 5 minutes with 75% bleach, and rinsed 3 times withdouble distilled H₂O, 5 min each.

Surface-sterilized seeds are placed on the callus induction mediumcontaining Murashige and Skoog basal salts and vitamins, 20 g/L sucrose,150 mg/L asparagine, 500 mg/L casein hydrolysate, 3 g/L Phytagel, 10mg/L BAP, and 5 mg/L dicamba. Plates are incubated in the dark at 25° C.for 4 weeks for seed germination and embryogenic callus induction.

After 4 weeks on the callus induction medium, the shoots and roots ofthe seedlings are trimmed away, the callus is transferred to freshmedia, maintained in culture for another 4 weeks, and then transferredto MSO medium in light for 2 weeks. Several pieces of callus (11-17weeks old) are either strained through a 10 mesh sieve and put ontocallus induction medium, or cultured in 100 ml of liquid ryegrass callusinduction media (same medium as for callus induction with agar) in a 250ml flask. The flask is wrapped in foil and shaken at 175 rpm in the darkat 23° C. for 1 week. Sieving the liquid culture with a 40-mesh sievecollected the cells. The fraction collected on the sieve is plated andcultured on solid ryegrass callus induction medium for 1 week in thedark at 25° C. The callus is then transferred to and cultured on MSmedium containing 1% sucrose for 2 weeks.

Transformation can be accomplished with either Agrobacterium of withparticle bombardment methods. An expression vector is created containinga constitutive plant promoter and the cDNA of the gene in a pUC vector.The plasmid DNA is prepared from E. coli cells using with Qiagen kitaccording to manufacturer's instruction. Approximately 2 g ofembryogenic callus is spread in the center of a sterile filter paper ina Petri dish. An aliquot of liquid MSO with 10 g/L sucrose is added tothe filter paper. Gold particles (1.0 μm in size) are coated withplasmid DNA according to method of Sanford et al., 1993 and delivered tothe embryogenic callus with the following parameters: 500 μg particlesand 2 μg DNA per shot, 1300 psi and a target distance of 8.5 cm fromstopping plate to plate of callus and 1 shot per plate of callus.

After the bombardment, calli are transferred back to the fresh callusdevelopment medium and maintained in the dark at room temperature for a1-week period. The callus is then transferred to growth conditions inthe light at 25° C. to initiate embryo differentiation with theappropriate selection agent, e.g. 250 nM Arsenal, 5 mg/L PPT or 50 mg/Lkanamycin. Shoots resistant to the selection agent are appearing andonce rotted are transferred to soil.

Samples of the primary transgenic plants (T0) are analyzed by PCR toconfirm the presence of T-DNA. These results are confirmed by Southernhybridization in which DNA is electrophoresed on a 1% agarose gel andtransferred to a positively charged nylon membrane (Roche Diagnostics).The PCR DIG Probe Synthesis Kit (Roche Diagnostics) is used to prepare adigoxigenin-labelled probe by PCR, and used as recommended by themanufacturer.

Transgenic T0 ryegrass plants are propagated vegetatively by excisingtillers. The transplanted tillers are maintained in the greenhouse for 2months until well established. The shoots are defoliated and allowed togrow for 2 weeks.

T1 or T2 generation plants are produced and are grown under therespective conditions (low temperature, drought conditions, N-limitedconditions, conditions in the absence of stress as well as nutrientdeficiencies), and for example subjected to experiments with limitednitrogen supply: Plants receive limited nitrogen supply by use of anutrient depleted soil. Nutrients apart from nitrogen are supplied by anutrient solution. For NUE assessment biomass production and/or drymatter production and/or seed yield is compared to non-transgenic wildtype plants. For the other traits the procedure is adapted accordingly.

EXAMPLE 5

Engineering soybean plants with increased yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction by over-expressing NUE related protein (NUERP) encoding genesfrom Saccharomyces cerevisiae or E. coli or by over-expressing NUErelated protein (NUERP) encoding genes from for example Brassica napus,Glycine max, Zea mays or Oryza sativa

Soybean is transformed according to the following modification of themethod described in the Texas A&M patent U.S. Pat. No. 5,164,310.Several commercial soybean varieties are amenable to transformation bythis method. The cultivar Jack (available from the Illinois SeedFoundation) is a commonly used for transformation. Seeds are sterilizedby immersion in 70% (v:v) ethanol for 6 min and in 25% commercial bleach(NaOCl) supplemented with 0.1% (v:v) Tween for 20 min, followed byrinsing 4 times with sterile double distilled water. Seven-day seedlingsare propagated by removing the radicle, hypocotyl and one cotyledon fromeach seedling. Then, the epicotyl with one cotyledon is transferred tofresh germination media in petri dishes and incubated at 25° C. under a16-h photoperiod (approx. 100 μE/m²s) for three weeks. Axillary nodes(approx. 4 mm in length) were cut from 3-4 week-old plants. Axillarynodes are excised and incubated in Agrobacterium LBA4404 culture.

Many different binary vector systems have been described for planttransformation (e.g. An G., in Agrobacterium Protocols. Methods inMolecular Biology Vol. 44, p. 47-62, Gartland K.M.A. and Davey M.R. eds.Humana Press, Totowa, N.J.). Many are based on the vector pBIN19described by Bevan (Nucleic Acid Research. 12, 8711 (1984)) thatincludes a plant gene expression cassette flanked by the left and rightborder sequences from the Ti plasmid of Agrobacterium tumefaciens. Aplant gene expression cassette consists of at least two genes—aselection marker gene and a plant promoter regulating the transcriptionof the cDNA or genomic DNA of the trait gene. Various selection markergenes can be used including the Arabidopsis gene encoding a mutatedacetohydroxy acid synthase (AHAS) enzyme (U.S. Pat. Nos. 5,7673,666 and6,225,105). Similarly, various promoters can be used to regulate thetrait gene to provide constitutive, developmental, tissue orenvironmental regulation of gene transcription. In this example, the 34Spromoter (GenBank Accession numbers M59930 and X16673) can be used toprovide constitutive expression of the trait gene.

After the co-cultivation treatment, the explants are washed andtransferred to selection media supplemented with 500 mg/L timentin.Shoots are excised and placed on a shoot elongation medium. Shootslonger than 1 cm are placed on rooting medium for two to four weeksprior to transplanting to soil.

The primary transgenic plants (T0) are analyzed by PCR to confirm thepresence of T-DNA. These results are confirmed by Southern hybridizationin which DNA is electrophoresed on a 1 agarose gel and transferred to apositively charged nylon membrane (Roche Diagnostics). The PCR DIG ProbeSynthesis Kit (Roche Diagnostics) is used to prepare adigoxigenin-labelled probe by PCR, and used as recommended by themanufacturer.

Soybean Plants Over-Expressing NUE-Related Genes from Brassica napus,Glycine Max, Zea Mays or Oryza sativa for Example have Higher SeedYields

T1 or T2 generation plants are produced and are grown under therespective conditions (low temperature, drought conditions, N-limitedconditions, conditions in the absence of stress as well as nutrientdeficiencies), and for example subjected to experiments with limitednitrogen supply: Plants receive limited nitrogen supply by use of anutrient depleted soil. Nutrients apart from nitrogen are supplied by anutrient solution. For NUE assessment biomass production and/or drymatter production and/or seed yield is compared to non-transgenic wildtype plants. For the other traits the procedure is adapted accordingly.

EXAMPLE 6

Engineering Rapeseed/Canola plants with increased yield, especiallyenhanced stress tolerance, preferably tolerance to low temperatureand/or tolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction, by over-expressing NUE related protein (NUERP) encodinggenes from Saccharomyces cerevisiae or E. coli or by over-expressing NUErelated protein (NUERP) encoding genes from for example Brassica napus,Glycine max, Zea mays or Oryza sativa

Cotyledonary petioles and hypocotyls of 5-6 day-old young seedlings areused as explants for tissue culture and transformed according to Babicet al. (Plant Cell Rep 17, 183 (1998)). The commercial cultivar Westar(Agriculture Canada) is the standard variety used for transformation,but other varieties can be used.

Agrobacterium tumefaciens LBA4404 containing a binary vector can be usedfor canola transformation. Many different binary vector systems havebeen described for plant transformation (e.g. An G., in AgrobacteriumProtocols. Methods in Molecular Biology Vol. 44, p. 47-62, GartlandK.M.A. and Davey M.R. eds. Humana Press, Totowa, N.J.). Many are basedon the vector pBIN19 described by Bevan (Nucleic Acid Research. 12, 8711(1984)) that includes a plant gene expression cassette flanked by theleft and right border sequences from the Ti plasmid of Agrobacteriumtumefaciens. A plant gene expression cassette consists of at least twogenes—a selection marker gene and a plant promoter regulating thetranscription of the cDNA or genomic DNA of the trait gene. Variousselection marker genes can be used including the Arabidopsis geneencoding a mutated acetohydroxy acid synthase (AHAS) enzyme (U.S. Pat.Nos. 5,7673,666 and 6,225,105). Similarly, various promoters can be usedto regulate the trait gene to provide constitutive, developmental,tissue or environmental regulation of gene transcription. In thisexample, the 34S promoter (GenBank Accession numbers M59930 and X16673)can be used to provide constitutive expression of the trait gene.

Canola seeds are surface-sterilized in 70% ethanol for 2 min., and thenin 30% Clorox with a drop of Tween-20 for 10 min, followed by threerinses with sterilized distilled water. Seeds are then germinated invitro 5 days on half strength MS medium without hormones, 1% sucrose,0.7% Phytagar at 23° C., 16 h light. The cotyledon petiole explants withthe cotyledon attached are excised from the in vitro seedlings, andinoculated with Agrobacterium by dipping the cut end of the petioleexplant into the bacterial suspension. The explants are then culturedfor 2 days on MSBAP-3 medium containing 3 mg/L BAP, 3% sucrose, 0.7%Phytagar at 23° C., 16 h light. After two days of co-cultivation withAgrobacterium, the petiole explants are transferred to MSBAP-3 mediumcontaining 3 mg/L BAP, cefotaxime, carbenicillin, or timentin (300 mg/L)for 7 days, and then cultured on MSBAP-3 medium with cefotaxime,carbenicillin, or timentin and selection agent until shoot regeneration.When the shoots were 5-10 mm in length, they are cut and transferred toshoot elongation medium (MSBAP-0.5, containing 0.5 mg/L BAP). Shoots ofabout 2 cm in length are transferred to the rooting medium (MSO) forroot induction.

Samples of the primary transgenic plants (T0) are analyzed by PCR toconfirm the presence of T-DNA. These results are confirmed by Southernhybridization in which DNA is electrophoresed on a 1 agarose gel andtransferred to a positively charged nylon membrane (Roche Diagnostics).The PCR DIG Probe Synthesis Kit (Roche Diagnostics) is used to prepare adigoxigenin-labelled probe by PCR, and used as recommended by themanufacturer.

The transgenic plants are then evaluated for their enhanced increasedyield, especially enhanced stress tolerance, preferably tolerance to lowtemperature and/or tolerance to drought conditions, and/or enhancednutrient use efficiency, in particular NUE and/or increased biomassproduction, according to the method described in Example 3. It is foundthat transgenic rapeseed/canola over-expressing NUE related protein(NUERP) encoding genes from Brassica napus, Glycine max, Zea mays orOryza sativa for example show an increase in yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction, compared to non-transgenic control plants.

T1 or T2 generation plants are produced and are grown under therespective conditions (low temperature, drought conditions, N-limitedconditions, conditions in the absence of stress as well as nutrientdeficiencies), and for example subjected to experiments with limitednitrogen supply: Plants receive limited nitrogen supply by use of anutrient depleted soil. Nutrients apart from nitrogen are supplied by anutrient solution. For NUE assessment biomass production and/or drymatter production and/or seed yield is compared to non-transgenic wildtype plants. For the other traits the procedure is adapted accordingly.

EXAMPLE 7

Engineering corn plants with increased yield, especially enhanced stresstolerance, preferably tolerance to low temperature and/or tolerance todrought conditions, and/or enhanced nutrient use efficiency, inparticular enhanced NUE and/or increased biomass production, byover-expressing NUE related protein (NUERP) encoding genes fromSaccharomyces cerevisiae or E. coli or by over-expressing NUE relatedprotein (NUERP) encoding genes from for example Brassica napus, Glycinemax, Zea mays or Oryza sativa

Transformation of maize (Zea Mays L.) is performed with a modificationof the method described by Ishida et al. (Nature Biotech 14745 (1996)).Transformation is genotype-dependent in corn and only specific genotypesare amenable to transformation and regeneration. The inbred line A188(University of Minnesota) or hybrids with A188 as a parent are goodsources of donor material for transformation (Fromm et al. Biotech 8,833 (1990)), but other genotypes can be used successfully as well. Earsare harvested from corn plants at approximately 11 days afterpollination (DAP) when the length of immature embryos is about 1 to 1.2mm. Immature embryos are co-cultivated with Agrobacterium tumefaciensthat carry “super binary” vectors and transgenic plants are recoveredthrough organogenesis. The super binary vector system of Japan Tobaccois described in WO patents WO 94/00977 and WO 95/06722. Vectors wereconstructed as described. Various selection marker genes can be usedincluding the maize gene encoding a mutated acetohydroxy acid synthase(AHAS) enzyme (U.S. Pat. No. 6,025,541). Similarly, various promoterscan be used to regulate the trait gene to provide constitutive,developmental, tissue or environmental regulation of gene transcription.In this example, the 34S promoter (GenBank Accession numbers M59930 andX16673) was used to provide constitutive expression of the trait gene.

Excised embryos are grown on callus induction medium, then maizeregeneration medium, containing an imidazolinone herbicide as aselection agent. The Petri plates are incubated in the light at 25° C.for 2-3 weeks, or until shoots develop. The green shoots are transferredfrom each embryo to maize rooting medium and incubated at 25° C. for 2-3weeks, until roots develop. The rooted shoots are transplanted to soilin the greenhouse. T1 seeds are produced from plants that exhibittolerance to the imidazolinone herbicides and which are PCR positive forthe transgenes.

The T1 transgenic plants are then evaluated for their increased yield,especially enhanced stress tolerance, preferably tolerance to lowtemperature and/or tolerance to drought conditions, and/or enhancednutrient use efficiency, in particular enhanced NUE and/or increasedbiomass production, according to the methods described in Example 3. TheT1 generation of single locus insertions of the T-DNA will segregate forthe transgene in a 3:1 ratio (more precisely in a 1:2:1 ratio). Thoseprogeny containing one or two copies of the transgene are tolerantregarding the imidazolinone herbicide, and exhibit an increase in yield,especially enhanced stress tolerance, preferably tolerance to lowtemperature and/or tolerance to drought conditions, and/or enhancednutrient use efficiency, in particular enhancement of NUE and/orincreased biomass production, than those progeny lacking the transgenes.

T1 or T2 generation plants are produced and are grown under therespective conditions (low temperature, drought conditions, N-limitedconditions, conditions in the absence of stress as well as nutrientdeficiencies), and for example subjected to experiments with limitednitrogen supply: Plants receive limited nitrogen supply by use of anutrient depleted soil. Nutrients apart from nitrogen are supplied by anutrient solution. For NUE assessment biomass production and/or drymatter production and/or seed yield is compared to non-transgenic wildtype plants. For the other traits the procedure is adapted accordingly.Homozygous T2 plants exhibited similar phenotypes. Hybrid plants (F1progeny) of homozygous transgenic plants and non-transgenic plants alsoexhibited an increase in yield, especially enhanced stress tolerance,preferably tolerance to low temperature and/or tolerance to droughtconditions, and/or enhanced nutrient use efficiency, in particularenhanced NUE efficiency.

EXAMPLE 8

Engineering wheat plants with increased yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction, by over-expressing NUE related protein (NUERP) encodinggenes from Saccharomyces cerevisiae or E. coli or by over-expressing NUErelated protein (NUERP) encoding genes from for example Brassica napus,Glycine max, Zea mays or Oryza sativa for example

Transformation of wheat is performed with the method described by Ishidaet al. (Nature Biotech. 14745 (1996)). The cultivar Bobwhite (availablefrom CYMMIT, Mexico) is commonly used in transformation. Immatureembryos are co-cultivated with Agrobacterium tumefaciens that carry“super binary” vectors, and transgenic plants are recovered throughorganogenesis. The super binary vector system of Japan Tobacco isdescribed in WO patents WO 94/00977 and WO 95/06722. Vectors wereconstructed as described. Various selection marker genes can be usedincluding the maize gene encoding a mutated acetohydroxy acid synthase(AHAS) enzyme (U.S. Pat. No. 6,025,541). Similarly, various promoterscan be used to regulate the trait gene to provide constitutive,developmental, tissue or environmental regulation of gene transcription.In this example, the 34S promoter (GenBank Accession numbers M59930 andX16673) was used to provide constitutive expression of the trait gene.

After incubation with Agrobacterium, the embryos are grown on callusinduction medium, then regeneration medium, containing an imidazolinoneherbicide as a selection agent. The Petri plates are incubated in thelight at 25° C. for 2-3 weeks, or until shoots develop. The green shootsare transferred from each embryo to rooting medium and incubated at 25°C. for 2-3 weeks, until roots develop. The rooted shoots aretransplanted to soil in the greenhouse. T1 seeds are produced fromplants that exhibit tolerance to the imidazolinone herbicides and whichare PCR positive for the transgenes.

The T1 transgenic plants are then evaluated for their increased yield,especially enhanced stress tolerance, preferably tolerance to lowtemperature and/or tolerance to drought conditions, and/or enhancednutrient use efficiency, in particular enhanced NUE and/or increasedbiomass production, according to the method described in the previousexample 2. The T1 generation of single locus insertions of the T-DNAwill segregate for the transgene in a 3:1 ratio (more precisely in a1:2:1 ratio). Those progeny containing one or two copies of thetransgene are tolerant regarding the imidazolinone herbicide, andexhibit an increase in yield, especially enhanced stress tolerance,preferably tolerance to low temperature and/or tolerance to droughtconditions, and/or enhanced nutrient use efficiency, in particular anenhanced NUE and/or increased biomass production, than those progenylacking the transgenes. Homozygous T2 plants exhibited similarphenotypes. Plants with an increase in yield, especially enhanced stresstolerance, preferably tolerance to low temperature and/or tolerance todrought conditions, and/or enhanced nutrient use efficiency, inparticular NUE, have increased biomass production and/or dry matterproduction and/or seed yield under the respective conditions, like lowtemperature, drought conditions, limited nitrogen supply when comparedto non-transgenic wild type plants. Also plants with higher yield, inthe absence of stress conditions as well as in the absence of nutrientdeficiencies, have increased biomass production and/or dry matterproduction and/or seed yield under the respective conditions.

EXAMPLE 9 Identification of Identical and Heterologous Genes

Gene sequences can be used to identify identical or heterologous genesfrom cDNA or genomic libraries. Identical genes (e.g. full-length cDNAclones) can be isolated via nucleic acid hybridization using for examplecDNA libraries. Depending on the abundance of the gene of interest,100,000 up to 1,000,000 recombinant bacteriophages are plated andtransferred to nylon membranes. After denaturation with alkali, DNA isimmobilized on the membrane by e.g. UV cross linking. Hybridization iscarried out at high stringency conditions. In aqueous solution,hybridization and washing is performed at an ionic strength of 1 M NaCland a temperature of 68° C. Hybridization probes are generated by e.g.radioactive (³²P) nick transcription labeling (High Prime, Roche,Mannheim, Germany). Signals are detected by autoradiography.

Partially identical or heterologous genes that are related but notidentical can be identified in a manner analogous to the above-describedprocedure using low stringency hybridization and washing conditions. Foraqueous hybridization, the ionic strength is normally kept at 1 M NaClwhile the temperature is progressively lowered from 68 to 42° C.

Isolation of gene sequences with homology (or sequenceidentity/similarity) only in a distinct domain of (for example 10-20amino acids) can be carried out by using synthetic radio labeledoligonucleotide probes. Radiolabeled oligonucleotides are prepared byphosphorylation of the 5-prime end of two complementary oligonucleotideswith T4 polynucleotide kinase. The complementary oligonucleotides areannealed and ligated to form concatemers. The double strandedconcatemers are than radiolabeled by, for example, nick transcription.Hybridization is normally performed at low stringency conditions usinghigh oligonucleotide concentrations.

Oligonucleotide Hybridization Solution:

6×SSC

0.01 M sodium phosphate

1 mM EDTA (pH 8)

0.5% SDS

100 μg/mL denatured salmon sperm DNA

0.1% nonfat dried milk

During hybridization, temperature is lowered stepwise to 5-10° C. belowthe estimated oligonucleotide T_(m) or down to room temperature followedby washing steps and autoradiography. Washing is performed with lowstringency such as 3 washing steps using 4×SSC. Further details aredescribed by Sambrook J. et al., 1989, “Molecular Cloning: A LaboratoryManual,” Cold Spring Harbor Laboratory Press or Ausubel F. M. et al.,1994, “Current Protocols in Molecular Biology,” John Wiley & Sons.

EXAMPLE 10 Identification of Identical Genes by Screening ExpressionLibraries with Antibodies

c-DNA clones can be used to produce recombinant polypeptide for examplein E. coli (e.g. Qiagen QIAexpress pQE system). Recombinant polypeptidesare then normally affinity purified via Ni-NTA affinity chromatography(Qiagen). Recombinant polypeptides are then used to produce specificantibodies for example by using standard techniques for rabbitimmunization. Antibodies are affinity purified using a Ni-NTA columnsaturated with the recombinant antigen as described by Gu et al.,BioTechniques 17, 257 (1994). The antibody can than be used to screenexpression cDNA libraries to identify identical or heterologous genesvia an immunological screening (Sambrook, J. et al., 1989, “MolecularCloning: A Laboratory Manual,” Cold Spring Harbor Laboratory Press orAusubel, F. M. et al., 1994, “Current Protocols in Molecular Biology”,John Wiley & Sons).

EXAMPLE 11 In Vivo Mutagenesis

In vivo mutagenesis of microorganisms can be performed by passage ofplasmid (or other vector) DNA through E. coli or other microorganisms(e.g. Bacillus spp. or yeasts such as Saccharomyces cerevisiae) whichare impaired in their capabilities to maintain the integrity of theirgenetic information. Typical mutator strains have mutations in the genesfor the DNA repair system (e.g., mutHLS, mutD, mutT, etc.; forreference, see Rupp W.D., DNA repair mechanisms, in: Escherichia coifand Salmonella, p. 2277-2294, ASM, 1996, Washington.) Such strains arewell known to those skilled in the art. The use of such strains isillustrated, for example, in Greener A. and Callahan M., Strategies 7,32 (1994). Transfer of mutated DNA molecules into plants is preferablydone after selection and testing in microorganisms. Transgenic plantsare generated according to various examples within the exemplificationof this document.

EXAMPLE 12

Engineering Arabidopsis plants with increased yield, especially enhancedstress tolerance, preferably tolerance to low temperature and/ortolerance to drought conditions, and/or enhanced nutrient useefficiency, in particular enhanced NUE and/or increased biomassproduction, by over-expressing NUERP encoding genes for example fromBrassica Napus, Glycine Max, Zea Mays or Oryza sativa usingtissue-specific promoters.

Transgenic Arabidopsis plants over-expressing NUE related protein(NUERP) encoding genes from Brassica napus, Glycine max, Zea mays andOryza sativa for example are created as described in example 1 toexpress the NUE related protein (NUERP) encoding transgenes under thecontrol of a tissue-specific promoter. T2 generation plants are producedand grown under N-limited conditions. Plants with an increase in yield,especially enhanced stress tolerance, preferably tolerance to lowtemperature and/or tolerance to drought conditions, and/or enhancednutrient use efficiency, in particular NUE, have increased biomassproduction and/or dry matter production and/or seed yield under therespective conditions, like low temperature, drought conditions, limitednitrogen supply when compared to non-transgenic wild type plants. Alsoplants with higher yield, in the absence of stress conditions as well asin the absence of nutrient deficiencies, have increased biomassproduction and/or dry matter production and/or seed yield under therespective conditions.

EXAMPLE 13

Engineering rice plants with increased yield, especially enhanced stresstolerance, preferably tolerance to low temperature and/or tolerance todrought conditions, and/or enhanced nutrient use efficiency, inparticular enhanced NUE and/or increased biomass production, byover-expressing NUE related protein (NUERP) encoding genes fromSaccharomyces cerevisiae or E. coli or by over-expressing NUE relatedprotein (NUERP) encoding genes from for example Brassica napus, Glycinemax, Zea mays or Oryza sativa

The Agrobacterium containing the expression vector of the invention isused to transform Oryza sativa plants. Mature dry seeds of the ricejaponica cultivar Nipponbare are dehusked. Sterilization is carried outby incubating for one minute in 70% ethanol, followed by 30 minutes in0.2% HgCl₂, followed by a 6 times 15 minutes wash with sterile distilledwater. The sterile seeds are then germinated on a medium containing2,4-D (callus induction medium). After incubation in the dark for fourweeks, embryogenic, scutellum-derived calli are excised and propagatedon the same medium. After two weeks, the calli are multiplied orpropagated by subculture on the same medium for another 2 weeks.Embryogenic callus pieces are sub-cultured on fresh medium 3 days beforeco-cultivation (to boost cell division activity).

Agrobacterium strain LBA4404 containing the expression vector of theinvention is used for co-cultivation. Agrobacterium is inoculated on ABmedium with the appropriate antibiotics and cultured for 3 days at 28°C. The bacteria are then collected and suspended in liquidco-cultivation medium to a density (OD600) of about 1. The suspension isthen transferred to a Petri dish and the calli immersed in thesuspension for 15 minutes. The callus tissues are then blotted dry on afilter paper and transferred to solidified, co-cultivation medium andincubated for 3 days in the dark at 25° C. Co-cultivated calli are grownon 2,4-D-containing medium for 4 weeks in the dark at 28° C. in thepresence of a selection agent. During this period, rapidly growingresistant callus islands developed. After transfer of this material to aregeneration medium and incubation in the light, the embryogenicpotential is released and shoots developed in the next four to fiveweeks. Shoots are excised from the calli and incubated for 2 to 3 weekson an auxin-containing medium from which they are transferred to soil.Hardened shoots are grown under high humidity and short days in agreenhouse.

Approximately 35 independent T0 rice transformants are generated for oneconstruct. The primary transformants are transferred from a tissueculture chamber to a greenhouse. After a quantitative PCR analysis toverify copy number of the T-DNA insert, only single copy transgenicplants that exhibit tolerance to the selection agent are kept forharvest of T1 seed. Seeds are then harvested three to five months aftertransplanting. The method yielded single locus transformants at a rateof over 50% (Aldemita and Hodges 1996, Chan et al. 1993, Hiei et al.1994).

For the cycling drought assay repetitive stress is applied to plantswithout leading to desiccation. The water supply throughout theexperiment is limited and plants are subjected to cycles of drought andre-watering. For measuring biomass production, plant fresh weight isdetermined one day after the final watering by cutting shoots andweighing them. At an equivalent degree of drought stress, tolerantplants are able to resume normal growth whereas susceptible plants havedied or suffer significant injury resulting in shorter leaves and lessdry matter.

For testing the other traits according to the present invention theprocedure is adapted accordingly.

FIGURES

FIG. 1 a Vector VC-MME220-1 SEQ ID NO 1 used for cloning gene ofinterest for non-targeted expression.

FIG. 1 b Vector VC-MME220-1 qcz SEQ ID NO 14389 used for cloning gene ofinterest for non-targeted expression.

FIG. 2 a Vector VC-MME221-1 SEQ ID NO: 2 used for cloning gene ofinterest for non-targeted expression.

FIG. 2 b Vector VC-MME221-1qcz SEQ ID NO 14390 used for cloning gene ofinterest for non-targeted expression.

FIG. 3 a Vector VC-MME354-1 SEQ ID NO: 3 used for cloning gene ofinterest for targeted expression.

FIG. 3 b Vector VC-MME354-1 QCZ SEQ ID NO 14391 used for cloning gene ofinterest for targeted expression.

FIG. 4 a Vector VC-MME432-1 SEQ ID NO: 5 used for cloning gene ofinterest for targeted expression.

FIG. 4 b Vector VC-MME432-1qcz SEQ ID NO 14393 used for cloning gene ofinterest for targeted expression.

FIG. 5 a Vector VC-MME489-1p SEQ ID NO 15 used for cloning gene ofinterest for non-targeted expression and cloning of a targetingsequence.

FIG. 5 b Vector VC-MME489-1QCZ SEQ ID NO 14395 used for cloning gene ofinterest for non-targeted expression and cloning of a targetingsequence.

FIG. 6 Vector pMTX0270p SEQ ID NO: 16 used for cloning of a targetingsequence.

In the sequence listing the so-called numeric identifier <223> referssome times to “transl_table=11”. This is a reference to rules oftranslation of the coding sequences mentioned in “the Genetic Code” Item11 “The Bacterial and Plant tissue Code (transl_table=11)” byncbi.nlm.nih.gov/Taxonomy/Utils/wprintgc.cgi.

TABLE IA Nucleic acid sequence ID numbers Ap- 5. pli- Lead ca- 1. 2. 3.4. SEQ 6. 7. tion Hit Project Locus Organism ID Target SEQ IDs ofNucleic Acid Homologs 1 1 NUE_OEX_1 B0017 E. coli   38 Cytoplasmic — 1 2NUE_OEX_1 B0045 E. coli   42 Cytoplasmic 44, 46, 48, 50, 52, 54, 56, 58,60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94,96 1 3 NUE_OEX_1 B0180 E. coli  123 Plastidic 125, 127, 129, 131, 133,135, 137, 139, 141, 143, 145, 147, 149, 151, 153, 155, 157, 159, 161,163, 165, 167, 169, 171, 173, 175, 177, 179, 181, 183, 185, 187, 189,191, 193, 195, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217,219, 221, 223, 225, 227, 229, 231, 233, 235, 237, 239, 241, 243, 245,247, 249, 251, 253, 255, 257, 259, 261, 263, 265, 267, 269, 271, 273,275, 277, 279, 281, 283, 285, 287, 289, 291, 293, 295, 297, 299, 301,303, 305, 307, 309, 311, 313, 315, 317, 319, 321, 323, 325, 327, 329,331, 333, 335, 337, 339, 341, 343, 345, 347, 349, 351, 353, 355, 357,359, 361, 363 1 4 NUE_OEX_1 B0242 E. coli  380 Plastidic 382, 384, 386,388, 390, 392, 394, 396, 398, 400, 402, 404, 406, 408, 410, 412, 414,416, 418, 420, 422, 424, 426, 428, 430, 432, 434, 436, 438, 440, 442,444, 446, 448, 450, 452, 454, 456, 458, 460, 462, 464, 466, 468, 470,472, 474, 476, 478, 480, 482, 484, 486, 488, 490, 492, 494, 496, 498,500, 502, 504, 506, 508, 510, 512, 514, 516, 518, 520, 522, 524, 526,528, 530, 532, 534, 536, 538, 540, 542, 544, 546, 548, 550, 552, 554,556, 558, 560, 562, 564, 566, 568, 570, 572, 574, 576, 578, 580, 582,584, 586, 588, 590, 592, 594, 596, 598, 600, 602, 604, 606, 608, 610,612, 614, 616, 618, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638,640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660 1 5 NUE_OEX_1B0403 E. coli  679 Plastidic 681, 683, 685, 687, 689, 691, 693, 695,697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723,725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751,753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779,781, 783, 785, 787, 789, 791, 793, 795, 797, 799 1 6 NUE_OEX_1 B0474 E.coli  812 Cytoplasmic 814, 816, 818, 820, 822, 824, 826, 828, 830, 832,834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860,862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888,890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916,918, 920, 922, 924, 926, 928, 930, 932, 934, 936, 938, 940, 942, 944,946, 948, 950, 952, 954, 956 1 7 NUE_OEX_1 B0754 E. coli  1055 Plastidic1057, 1059, 1061, 1063, 1065, 1067, 1069, 1071, 1073, 1075, 1077, 1079,1081, 1083, 1085, 1087, 1089, 1091, 1093, 1095, 1097, 1099, 1101, 1103,1105, 1107, 1109, 1111, 1113, 1115, 1117, 1119, 1121, 1123, 1125, 1127,1129, 1131, 1133, 1135, 1137, 1139, 1141, 1143, 1145, 1147, 1149, 1151,1153, 1155, 1157, 1159, 1161, 1163, 1165, 1167, 1169, 1171, 1173, 1175,1177, 1179, 1181, 1183, 1185, 1187, 1189, 1191, 1193, 1195, 1197, 1199,1201, 1203, 1205, 1207, 1209, 1211, 1213, 1215, 1217, 1219, 1221, 1223,1225, 1227, 1229, 1231, 1233, 1235, 1237, 1239, 1241, 1243, 1245, 1247,1249, 1251, 1253, 1255, 1257, 1259, 1261, 1263, 1265, 1267, 1269, 1271,1273, 1275, 1277, 1279, 1281, 1283, 1285, 1287, 1289, 1291, 1293, 1295,1297, 1299, 1301, 1303, 1305, 1307, 1309, 1311, 1313, 1315, 1317, 1319,1321, 1323, 1325, 1327, 1329, 1331, 1333, 1335, 1337, 1339, 1341, 1343,1345, 1347, 1349, 1351, 1353, 1355, 1357, 1359, 1361, 1363, 1365, 1367,1369, 1371, 1373, 1375, 1377, 1379, 1381, 1383, 1385, 1387, 1389, 1391,1393, 1395, 1397, 1399, 1401, 1403, 1405, 1407, 1409, 1411, 1413, 1415,1417, 1419, 1421, 1423, 1425, 1427, 1429, 1431, 1433, 1435, 1437, 1439,1441, 1443, 1445, 1447, 1449, 1451, 1453, 1455, 1457, 1459, 1461, 1463,1465, 1467, 1469, 1471, 1473, 1475, 1477, 1479, 1481, 1483, 1485, 1487,1489, 1491, 1493, 1495, 1497, 1499, 1501, 1503, 1505, 1507, 1509, 1511,1513, 1515, 1517, 1519, 1521, 1523, 1525, 1527, 1529, 1531, 1533, 1535,1537, 1539, 1541, 1543, 1545, 1547, 1549 1 8 NUE_OEX_1 B0784 E. coli 1563 Cytoplasmic 1565, 1567, 1569, 1571, 1573, 1575, 1577, 1579, 1581,1583, 1585, 1587, 1589, 1591, 1593, 1595, 1597, 1599, 1601, 1603, 1605,1607, 1609, 1611, 1613, 1615, 1617, 1619, 1621, 1623, 1625, 1627, 1629,1631, 1633, 1635, 1637, 1639, 1641, 1643, 1645, 1647, 1649, 1651, 1653,1655, 1657, 1659, 1661, 1663, 1665, 1667, 1669, 1671, 1673, 1675, 1677,1679, 1681, 1683, 1685, 1687, 1689, 1691, 1693, 1695, 1697, 1699 1 9NUE_OEX_1 B0873 E. coli  1705 Plastidic 1707, 1709, 1711, 1713, 1715,1717, 1719, 1721, 1723, 1725, 1727, 1729, 1731, 1733, 1735, 1737, 1739,1741, 1743, 1745, 1747, 1749, 1751, 1753, 1755, 1757, 1759, 1761, 1763,1765, 1767, 1769, 1771, 1773, 1775, 1777, 1779, 1781, 1783, 1785, 1787,1789, 1791, 1793, 1795, 1797, 1799, 1801, 1803, 1805, 1807, 1809, 1811,1813, 1815, 1817, 1819, 1821, 1823, 1825, 1827, 1829 1 10 NUE_OEX_1B1014 E. coli  1844 Cytoplasmic 1846, 1848, 1850, 1852, 1854, 1856,1858, 1860, 1862, 1864, 1866, 1868, 1870, 1872, 1874, 1876, 1878, 1880,1882, 1884, 1886, 1888, 1890, 1892, 1894, 1896, 1898, 1900, 1902, 1904,1906, 1908, 1910, 1912, 1914, 1916, 1918, 1920, 1922, 1924, 1926, 1928,1930 1 11 NUE_OEX_1 B1020 E. coli  1950 Plastidic 1952, 1954, 1956,1958, 1960, 1962, 1964 1 12 NUE_OEX_1 B1180 E. coli  1975 Cytoplasmic1977, 1979, 1981, 1983, 1985, 1987, 1989, 1991, 1993, 1995, 1997, 1999,2001, 2003, 2005, 2007, 2009, 2011, 2013, 2015, 2017, 2019, 2021, 2023,2025, 2027, 2029, 2031, 2033, 2035, 2037, 2039, 2041, 2043, 2045, 2047,2049, 2051, 2053, 2055, 2057, 2059, 2061, 2063, 2065, 2067, 2069, 2071,2073, 2075, 2077, 2079, 2081, 2083, 2085, 2087, 2089, 2091, 2093, 2095,2097 1 13 NUE_OEX_1 B1933 E. coli  2127 Plastidic 2129, 2131 1 14NUE_OEX_1 B2032 E. coli  2135 Plastidic 2137, 2139, 2141, 2143, 2145,2147, 2149, 2151, 2153, 2155, 2157, 2159, 2161, 2163, 2165 1 15NUE_OEX_1 B2165 E. coli  2171 Plastidic 2173, 2175, 2177, 2179, 2181,2183, 2185, 2187, 2189, 2191, 2193, 2195, 2197, 2199, 2201, 2203, 2205,2207, 2209, 2211, 2213, 2215, 2217, 2219, 2221, 2223, 2225, 2227, 2229,2231, 2233, 2235, 2237, 2239, 2241, 2243, 2245, 2247, 2249, 2251, 2253,2255, 2257, 2259, 2261, 2263, 2265, 2267, 2269, 2271, 2273, 2275, 2277,2279, 2281, 2283 1 16 NUE_OEX_1 B2223 E. coli  2297 Plastidic 2299,2301, 2303, 2305, 2307, 2309, 2311, 2313, 2315, 2317, 2319, 2321, 2323,2325, 2327, 2329, 2331, 2333, 2335, 2337, 2339, 2341, 2343, 2345, 2347,2349, 2351, 2353, 2355, 2357, 2359, 2361, 2363, 2365, 2367, 2369, 2371,2373, 2375, 2377, 2379, 2381, 2383, 2385, 2387, 2389, 2391, 2393, 2395,2397, 2399, 2401, 2403, 2405, 2407, 2409, 2411, 2413, 2415, 2417 1 17NUE_OEX_1 B2238 E. coli  2426 Plastidic 2428, 2430, 2432, 2434, 2436,2438, 2440, 2442 1 17 NUE_OEX_1 B2238 E. coli  2426 Cytoplasmic 2428,2430, 2432, 2434, 2436, 2438, 2440, 2442 1 18 NUE_OEX_1 B2310 E. coli 2452 Plastidic 2454, 2456, 2458, 2460, 2462, 2464, 2466, 2468, 2470,2472, 2474, 2476, 2478, 2480, 2482, 2484, 2486, 2488, 2490, 2492, 2494,2496, 2498, 2500, 2502, 2504, 2506, 2508, 2510, 2512, 2514, 2516, 2518,2520, 2522, 2524, 2526, 2528, 2530, 2532, 2534, 2536, 2538, 2540, 2542 119 NUE_OEX_1 B2431 E. coli  2551 Plastidic 2553, 2555, 2557, 2559, 2561,2563, 2565, 2567, 2569, 2571, 2573, 2575, 2577, 2579, 2581, 2583, 2585,2587, 2589 1 20 NUE_OEX_1 B2600 E. coli  2600 Plastidic 2602, 2604,2606, 2608, 2610, 2612, 2614, 2616, 2618, 2620, 2622, 2624, 2626, 2628,2630, 2632, 2634, 2636, 2638, 2640, 2642, 2644, 2646, 2648, 2650, 2652,2654, 2656 1 21 NUE_OEX_1 B2766 E. coli  2668 Plastidic 2670, 2672,2674, 2676, 2678, 2680, 2682, 2684, 2686, 2688, 2690, 2692, 2694, 2696,2698, 2700, 2702, 2704, 2706, 2708, 2710, 2712, 2714, 2716, 2718, 2720,2722, 2724, 2726, 2728, 2730, 2732, 2734, 2736, 2738, 2740, 2742, 2744,2746, 2748, 2750, 2752, 2754, 2756, 2758, 2760, 2762, 2764 1 22NUE_OEX_1 B2903 E. coli  2772 Cytoplasmic 2774, 2776, 2778, 2780, 2782,2784, 2786, 2788, 2790, 2792, 2794, 2796, 2798, 2800, 2802, 2804, 2806,2808, 2810, 2812, 2814, 2816, 2818, 2820, 2822, 2824, 2826, 2828, 2830,2832, 2834, 2836, 2838, 2840, 2842, 2844, 2846, 2848, 2850, 2852, 2854,2856, 2858, 2860, 2862, 2864, 2866, 2868, 2870, 2872, 2874, 2876, 2878,2880, 2882, 2884, 2886, 2888, 2890, 2892, 2894, 2896, 2898, 2900, 2902,2904, 2906, 2908, 2910, 2912, 2914, 2916, 2918, 2920, 2922, 2924, 2926,2928, 2930, 2932, 2934, 2936, 2938, 2940, 2942, 2944, 2946, 2948, 2950,2952, 2954, 2956, 2958, 2960, 2962, 2964, 2966, 2968, 2970, 2972, 2974,2976, 2978, 2980, 2982, 2984, 2986, 2988, 2990, 2992, 2994, 2996, 2998,3000, 3002, 3004, 3006, 3008, 3010, 3012, 3014, 3016, 3018, 3020, 3022,3024, 3026, 3028, 3030, 3032, 3034, 3036, 3038, 3040, 3042, 3044, 3046,3048, 3050, 3052, 3054, 3056, 3058, 3060, 3062, 3064, 3066, 3068, 3070,3072, 3074, 3076, 3078, 3080, 3082, 3084, 3086, 3088, 3090, 3092, 3094 123 NUE_OEX_1 B3117 E. coli  3117 Plastidic 3119, 3121, 3123, 3125, 3127,3129, 3131, 3133, 3135, 3137, 3139, 3141, 3143, 3145, 3147, 3149, 3151,3153, 3155, 3157, 3159, 3161, 3163, 3165, 3167, 3169, 3171, 3173, 3175,3177, 3179, 3181, 3183, 3185, 3187, 3189, 3191, 3193, 3195, 3197, 3199,3201, 3203, 3205, 3207, 3209, 3211, 3213, 3215, 3217, 3219, 3221, 3223,3225, 3227, 3229, 3231, 3233, 3235, 3237, 3239, 3241, 3243, 3245, 3247,3249, 3251, 3253, 3255, 3257, 3259, 3261, 3263, 3265, 3267, 3269, 3271,3273, 3275, 3277, 3279, 3281, 3283, 3285, 3287, 3289, 3291, 3293, 3295,3297, 3299, 3301, 3303, 3305, 3307, 3309, 3311, 3313, 3315, 3317, 3319,3321, 3323, 3325, 3327, 3329, 3331, 3333, 3335, 3337, 3339, 3341, 3343,3345, 3347, 3349, 3351, 3353, 3355, 3357, 3359, 3361, 3363, 3365, 3367,3369, 3371 1 24 NUE_OEX_1 B3120 E. coli  3390 Plastidic 3392 1 25NUE_OEX_1 B3216 E. coli  3396 Plastidic 3398, 3400, 3402, 3404, 3406,3408, 3410, 3412, 3414, 3416, 3418, 3420, 3422, 3424, 3426, 3428, 3430,3432, 3434, 3436, 3438, 3440, 3442, 3444, 3446, 3448, 3450, 3452, 3454,3456, 3458, 3460, 3462, 3464 1 26 NUE_OEX_1 B3451 E. coli  3470Plastidic 3472, 3474, 3476, 3478, 3480, 3482, 3484, 3486, 3488, 3490,3492, 3494, 3496, 3498, 3500, 3502, 3504, 3506, 3508, 3510, 3512, 3514,3516, 3518, 3520, 3522, 3524, 3526, 3528, 3530, 3532, 3534, 3536, 3538,3540, 3542, 3544, 3546, 3548, 3550, 3552, 3554 1 27 NUE_OEX_1 B3791 E.coli  3563 Cytoplasmic 3565, 3567, 3569, 3571, 3573, 3575, 3577, 3579,3581, 3583, 3585, 3587, 3589, 3591, 3593, 3595, 3597, 3599, 3601, 3603,3605, 3607, 3609, 3611, 3613, 3615, 3617, 3619, 3621, 3623, 3625, 3627,3629, 3631, 3633, 3635, 3637, 3639, 3641, 3643, 3645, 3647, 3649, 3651,3653, 3655, 3657, 3659, 3661, 3663, 3665, 3667, 3669, 3671, 3673, 3675,3677, 3679, 3681, 3683, 3685, 3687, 3689, 3691, 3693, 3695, 3697, 3699,3701, 3703, 3705, 3707, 3709, 3711, 3713, 3715, 3717, 3719, 3721, 3723,3725, 3727, 3729, 3731, 3733, 3735, 3737, 3739, 3741, 3743, 3745, 3747,3749, 3751, 3753, 3755, 3757, 3759, 3761, 3763 1 28 NUE_OEX_1 B3825 E.coli  3770* Plastidic 3772, 3774, 3776, 3778, 3780, 3782, 3784, 3786,3788, 3790, 3792, 3794, 3796, 3798, 3800, 3802, 3804, 3806, 3808, 3810,3812, 3814, 3816, 3818, 3820, 3822, 3824, 3826, 3828, 3830, 3832, 3834,3836, 3838, 3840, 3842, 3844, 3846, 3848, 3850, 3852, 3854, 3856, 3858,3860, 3862 1 29 NUE_OEX_1 YAL019W S. cerevisiae  3868 Cytoplasmic 3870,3872, 3874, 3876 1 30 NUE_OEX_1 YAR035W S. cerevisiae  3895 Cytoplasmic3897, 3899, 3901, 3903, 3905, 3907, 3909, 3911, 3913, 3915, 3917, 3919,3921, 3923, 3925, 3927, 3929, 3931, 3933, 3935, 3937, 3939 1 31NUE_OEX_1 YBL021C S. cerevisiae  3953 Cytoplasmic 3955, 3957, 3959,3961, 3963, 3965, 3967, 3969, 3971, 3973, 3975, 3977, 3979, 3981, 3983,3985, 3987, 3989, 3991, 3993, 3995, 3997, 3999, 4001, 4003, 4005, 4007,4009, 4011, 4013, 4015, 4017, 4019, 4021, 4023, 4025, 4027, 4029 1 32NUE_OEX_1 YBR055C S. cerevisiae  4111 Cytoplasmic 4113, 4115, 4117,4119, 4121, 4123, 4125, 4127, 4129, 4131, 4133, 4135, 4137, 4139 1 33NUE_OEX_1 YBR128C S. cerevisiae  4149 Cytoplasmic 4151, 4153, 4155 1 34NUE_OEX_1 YBR159W S. cerevisiae  4162 Cytoplasmic 4164, 4166, 4168,4170, 4172, 4174, 4176, 4178, 4180, 4182, 4184, 4186, 4188, 4190, 4192,4194, 4196, 4198, 4200, 4202, 4204, 4206, 4208, 4210, 4212 1 35NUE_OEX_1 YBR243C S. cerevisiae  4235 Cytoplasmic 4237, 4239, 4241,4243, 4245, 4247, 4249, 4251, 4253, 4255, 4257, 4259, 4261, 4263, 4265 135 NUE_OEX_1 YBR243C S. cerevisiae  4235 Plastidic 4237, 4239, 4241,4243, 4245, 4247, 4249, 4251, 4253, 4255, 4257, 4259, 4261, 4263, 4265 136 NUE_OEX_1 YBR262C S. cerevisiae  4280 Cytoplasmic 4282, 4284 1 37NUE_OEX_1 YCR019W S. cerevisiae  4288 Cytoplasmic 4290, 4292, 4294,4296, 4298, 4300, 4302, 4304 1 38 NUE_OEX_1 YDR070C S. cerevisiae  4315Cytoplasmic 4317, 4319 1 39 NUE_OEX_1 YDR079W S. cerevisiae  4325Cytoplasmic 4327, 4329 1 40 NUE_OEX_1 YDR123C S. cerevisiae  4335Cytoplasmic 4337, 4339 1 41 NUE_OEX_1 YDR137W S. cerevisiae  4346Cytoplasmic 4348, 4350 1 42 NUE_OEX_1 YDR294C S. cerevisiae  4361Cytoplasmic 4363, 4365, 4367, 4369, 4371, 4373, 4375, 4377, 4379, 4381,4383, 4385, 4387, 4389 1 42 NUE_OEX_1 YDR294C S. cerevisiae  4361Plastidic 4363, 4365, 4367, 4369, 4371, 4373, 4375, 4377, 4379, 4381,4383, 4385, 4387, 4389 1 43 NUE_OEX_1 YDR330W S. cerevisiae  4402Cytoplasmic 4404, 4406, 4408, 4410, 4412, 4414, 4416, 4418, 4420, 4422 144 NUE_OEX_1 YDR355C S. cerevisiae  4431 Cytoplasmic — 1 45 NUE_OEX_1YDR430C S. cerevisiae  4435 Plastidic 4437, 4439, 4441, 4443, 4445,4447, 4449, 4451, 4453, 4455, 4457, 4459, 4461, 4463, 4465, 4467 1 46NUE_OEX_1 YDR472W S. cerevisiae  4485 Cytoplasmic 4487, 4489, 4491,4493, 4495 1 47 NUE_OEX_1 YDR497C S. cerevisiae  4506 Plastidic 4508,4510, 4512, 4514, 4516, 4518, 4520, 4522, 4524, 4526, 4528, 4530, 4532,4534, 4536, 4538, 4540, 4542, 4544, 4546, 4548, 4550, 4552, 4554, 4556,4558, 4560, 4562, 4564, 4566, 4568, 4570, 4572, 4574, 4576, 4578, 4580,4582, 4584, 4586, 4588, 4590, 4592, 4594, 4596, 4598, 4600, 4602, 4604,4606, 4608, 4610, 4612, 4614, 4616, 4618, 4620, 4622, 4624, 4626, 4628,4630, 4632, 4634, 4636, 4638, 4640, 4642, 4644, 4646, 4648, 4650, 4652,4654, 4656, 4658, 4660, 4662, 4664, 4666, 4668, 4670, 4672, 4674, 4676,4678, 4680, 4682, 4684, 4686, 4688, 4690, 4692, 4694, 4696, 4698, 4700,4702, 4704, 4706, 4708, 4710, 4712, 4714, 4716, 4718, 4720, 4722, 4724,4726, 4728, 4730, 4732, 4734, 4736 1 48 NUE_OEX_1 YER029C S. cerevisiae 4790 Cytoplasmic 4792, 4794, 4796, 4798 1 49 NUE_OEX_1 YFR007W S.cerevisiae  4806 Cytoplasmic 4808, 4810, 4812, 4814, 4816, 4818, 4820,4822, 4824, 4826, 4828 1 50 NUE_OEX_1 YGL039W S. cerevisiae  4836Cytoplasmic 4838, 4840, 4842, 4844, 4846, 4848, 4850, 4852, 4854, 4856,4858, 4860, 4862, 4864, 4866, 4868, 4870, 4872, 4874, 4876, 4878, 4880,4882, 4884, 4886, 4888, 4890, 4892, 4894, 4896, 4898, 4900, 4902, 4904,4906, 4908, 4910, 4912, 4914, 4916, 4918, 4920, 4922, 4924, 4926, 4928,4930, 4932, 4934, 4936, 4938, 4940, 4942, 4944, 4946, 4948, 4950, 4952,4954, 4956, 4958, 4960, 4962, 4964, 4966, 4968, 4970, 4972, 4974, 4976,4978, 4980, 4982, 4984, 4986, 4988, 4990, 4992, 4994, 4996, 4998, 5000,5002, 5004, 5006, 5008, 5010, 5012, 5014, 5016, 5018, 5020, 5022, 5024,5026, 5028, 5030, 5032, 5034, 5036, 5038, 5040, 5042, 5044, 5046, 5048,5050, 5052, 5054, 5056, 5058, 5060, 5062, 5064, 5066, 5068, 5070, 5072,5074, 5076, 5078, 5080, 5082, 5084, 5086, 5088, 5090, 5092, 5094, 5096,5098, 5100, 5102, 5104, 5106, 5108, 5110, 5112, 5114, 5116, 5118, 5120,5122, 5124, 5126, 5128, 5130, 5132, 5134, 5136, 5138, 5140, 5142, 5144,5146, 5148, 5150, 5152, 5154, 5156, 5158, 5160, 5162, 5164, 5166, 5168,5170, 5172, 5174, 5176, 5178, 5180, 5182, 5184, 5186, 5188, 5190, 5192,5194, 5196, 5198, 5200, 5202, 5204, 5206, 5208, 5210, 5212 1 51NUE_OEX_1 YGL043W S. cerevisiae  5311 Cytoplasmic 5313, 5315, 5317,5319, 5321, 5323, 5325, 5327, 5329, 5331, 5333 1 52 NUE_OEX_1 YGR088W S.cerevisiae  5346 Cytoplasmic 5348, 5350, 5352, 5354, 5356, 5358, 5360,5362, 5364, 5366, 5368, 5370, 5372, 5374, 5376, 5378, 5380, 5382, 5384,5386, 5388, 5390, 5392, 5394, 5396, 5398, 5400, 5402, 5404, 5406, 5408,5410, 5412, 5414, 5416, 5418, 5420, 5422, 5424, 5426, 5428, 5430, 5432,5434, 5436, 5438, 5440, 5442, 5444, 5446, 5448, 5450, 5452, 5454, 5456,5458, 5460, 5462, 5464, 5466, 5468, 5470, 5472, 5474, 5476, 5478, 5480,5482, 5484, 5486, 5488, 5490, 5492, 5494, 5496, 5498, 5500, 5502, 5504,5506, 5508, 5510, 5512, 5514, 5516, 5518, 5520, 5522 1 53 NUE_OEX_1YGR122C-A S. cerevisiae  5533 Cytoplasmic 5535, 5537, 5539, 5541, 5543,5545 1 54 NUE_OEX_1 YGR142W S. cerevisiae  5551 Cytoplasmic 5553, 5555 155 NUE_OEX_1 YGR143W S. cerevisiae  5559 Cytoplasmic 5561, 5563, 5565,5567, 5569, 5571, 5573, 5575, 5577, 5579, 5581, 5583, 5585 1 56NUE_OEX_1 YGR165W S. cerevisiae  5602 Cytoplasmic 5604 1 57 NUE_OEX_1YGR170W S. cerevisiae  5608 Cytoplasmic 5610 1 58 NUE_OEX_1 YGR202C S.cerevisiae  5614 Cytoplasmic 5616, 5618, 5620, 5622, 5624, 5626, 5628,5630, 5632, 5634, 5636, 5638, 5640, 5642, 5644, 5646, 5648, 5650, 5652,5654, 5656, 5658 1 59 NUE_OEX_1 YGR266W S. cerevisiae  5666 Cytoplasmic5668, 5670, 5672, 5674, 5676, 5678, 5680, 5682, 5684, 5686 1 60NUE_OEX_1 YGR282C S. cerevisiae  5701 Cytoplasmic 5703, 5705, 5707,5709, 5711, 5713, 5715, 5717, 5719, 5721, 5723, 5725, 5727, 5729, 5731,5733, 5735, 5737, 5739 1 61 NUE_OEX_1 YGR290W S. cerevisiae  5750Cytoplasmic — 1 62 NUE_OEX_1 YHL021C S. cerevisiae  5754 Cytoplasmic5756, 5758, 5760, 5762, 5764, 5766, 5768 1 63 NUE_OEX_1 YHL031C S.cerevisiae  5778 Cytoplasmic 5780, 5782, 5784, 5786, 5788, 5790, 5792,5794, 5796, 5798, 5800, 5802, 5804, 5806 1 64 NUE_OEX_1 YHR011W S.cerevisiae  5812 Cytoplasmic 5814, 5816, 5818, 5820, 5822, 5824, 5826,5828, 5830, 5832, 5834, 5836, 5838, 5840, 5842, 5844, 5846, 5848, 5850,5852, 5854, 5856, 5858, 5860, 5862, 5864, 5866, 5868, 5870, 5872, 5874,5876, 5878, 5880, 5882, 5884, 5886, 5888, 5890, 5892, 5894, 5896, 5898,5900, 5902, 5904, 5906, 5908, 5910, 5912, 5914, 5916, 5918, 5920, 5922,5924, 5926, 5928, 5930, 5932, 5934, 5936, 5938, 5940, 5942, 5944, 5946,5948, 5950, 5952 1 65 NUE_OEX_1 YHR127W S. cerevisiae  5967 Cytoplasmic5969 1 66 NUE_OEX_1 YHR137W S. cerevisiae  5973 Cytoplasmic 5975, 5977,5979, 5981, 5983, 5985, 5987, 5989, 5991, 5993, 5995, 5997, 5999, 6001,6003, 6005, 6007, 6009, 6011, 6013, 6015, 6017, 6019 1 66 NUE_OEX_1YHR137W S. cerevisiae  5973 Plastidic 5975, 5977, 5979, 5981, 5983,5985, 5987, 5989, 5991, 5993, 5995, 5997, 5999, 6001, 6003, 6005, 6007,6009, 6011, 6013, 6015, 6017, 6019 1 67 NUE_OEX_1 YIL099W S. cerevisiae 6027 Cytoplasmic 6029, 6031, 6033, 6035, 6037, 6039, 6041, 6043, 6045,6047, 6049, 6051, 6053, 6055, 6057, 6059, 6061, 6063, 6065, 6067, 6069,6071, 6073, 6075, 6077, 6079, 6081, 6083, 6085, 6087, 6089, 6091, 6093,6095, 6097 1 67 NUE_OEX_1 YIL099W S. cerevisiae  6027 Plastidic 6029,6031, 6033, 6035, 6037, 6039, 6041, 6043, 6045, 6047, 6049, 6051, 6053,6055, 6057, 6059, 6061, 6063, 6065, 6067, 6069, 6071, 6073, 6075, 6077,6079, 6081, 6083, 6085, 6087, 6089, 6091, 6093, 6095, 6097 1 68NUE_OEX_1 YIL147C S. cerevisiae  6107 Cytoplasmic 6109, 6111, 6113,6115, 6117, 6119, 6121, 6123, 6125, 6127, 6129, 6131 1 69 NUE_OEX_1YIR034C S. cerevisiae  6150* Cytoplasmic 6152, 6154, 6156, 6158, 6160,6162, 6164, 6166, 6168, 6170, 6172, 6174, 6176, 6178, 6180, 6182, 6184 170 NUE_OEX_1 YJL013C S. cerevisiae  6198 Cytoplasmic 6200, 6202, 6204 171 NUE_OEX_1 YJL041W S. cerevisiae  6208 Cytoplasmic 6210, 6212, 6214,6216, 6218, 6220, 6222, 6224, 6226, 6228, 6230, 6232, 6234 1 72NUE_OEX_1 YJL064W S. cerevisiae  6242 Cytoplasmic — 1 73 NUE_OEX_1YJL067W S. cerevisiae  6246 Cytoplasmic — 1 74 NUE_OEX_1 YJL094C S.cerevisiae  6250 Cytoplasmic 6252, 6254, 6256, 6258, 6260, 6262, 6264,6266, 6268, 6270, 6272, 6274, 6276, 6278, 6280, 6282, 6284 1 75NUE_OEX_1 YJL171C S. cerevisiae  6297 Cytoplasmic 6299, 6301, 6303,6305, 6307, 6309, 6311, 6313, 6315 1 76 NUE_OEX_1 YJL213W S. cerevisiae 6326 Cytoplasmic 6328, 6330, 6332, 6334, 6336, 6338, 6340, 6342, 6344,6346, 6348, 6350, 6352, 6354, 6356, 6358, 6360, 6362, 6364, 6366, 6368,6370, 6372, 6374, 6376, 6378, 6380, 6382, 6384, 6386, 6388, 6390, 6392,6394, 6396, 6398, 6400, 6402, 6404, 6406, 6408, 6410, 6412, 6414, 6416,6418, 6420, 6422, 6424, 6426, 6428, 6430, 6432, 6434, 6436, 6438, 6440,6442, 6444, 6446, 6448, 6450, 6452, 6454, 6456, 6458, 6460, 6462, 6464,6466, 6468, 6470, 6472, 6474, 6476, 6478, 6480 1 77 NUE_OEX_1 YJR017C S.cerevisiae  6488 Cytoplasmic 6490, 6492, 6494, 6496, 6498, 6500, 6502,6504, 6506, 6508, 6510, 6512, 6514, 6516, 6518, 6520, 6522, 6524, 6526,6528, 6530, 6532, 6534, 6536, 6538, 6540 1 78 NUE_OEX_1 YJR058C S.cerevisiae  6550 Cytoplasmic 6552, 6554, 6556, 6558, 6560, 6562, 6564,6566, 6568, 6570, 6572, 6574, 6576, 6578, 6580, 6582, 6584, 6586, 6588,6590, 6592, 6594, 6596, 6598, 6600, 6602, 6604, 6606, 6608, 6610, 6612,6614, 6616, 6618, 6620, 6622, 6624, 6626, 6628, 6630, 6632, 6634, 6636,6638, 6640, 6642, 6644, 6646, 6648, 6650, 6652, 6654, 6656, 6658, 6660 179 NUE_OEX_1 YJR117W S. cerevisiae  6700 Cytoplasmic 6702, 6704, 6706,6708, 6710, 6712, 6714, 6716, 6718, 6720, 6722, 6724, 6726, 6728, 6730,6732, 6734, 6736, 6738, 6740, 6742, 6744, 6746, 6748, 6750, 6752, 6754,6756, 6758, 6760, 6762, 6764, 6766, 6768, 6770, 6772, 6774, 6776, 6778,6780, 6782, 6784, 6786, 6788 1 80 NUE_OEX_1 YJR121W S. cerevisiae  6816Cytoplasmic 6818, 6820, 6822, 6824, 6826, 6828, 6830, 6832, 6834, 6836,6838, 6840, 6842, 6844, 6846, 6848, 6850, 6852, 6854, 6856, 6858, 6860,6862, 6864, 6866, 6868, 6870, 6872, 6874, 6876, 6878, 6880, 6882, 6884,6886, 6888, 6890, 6892, 6894, 6896, 6898, 6900, 6902, 6904, 6906, 6908,6910, 6912, 6914, 6916, 6918, 6920, 6922, 6924, 6926, 6928, 6930, 6932,6934, 6936, 6938, 6940, 6942, 6944, 6946, 6948, 6950, 6952, 6954, 6956,6958, 6960, 6962, 6964, 6966, 6968, 6970, 6972, 6974, 6976, 6978, 6980,6982, 6984, 6986, 6988, 6990, 6992, 6994, 6996, 6998, 7000, 7002, 7004,7006, 7008, 7010, 7012, 7014, 7016, 7018, 7020, 7022, 7024, 7026, 7028,7030, 7032, 7034, 7036, 7038, 7040, 7042, 7044, 7046, 7048, 7050, 7052,7054, 7056, 7058, 7060, 7062, 7064, 7066, 7068, 7070, 7072, 7074, 7076,7078, 7080, 7082, 7084, 7086, 7088, 7090, 7092, 7094, 7096, 7098, 7100,7102, 7104, 7106, 7108, 7110, 7112, 7114, 7116, 7118, 7120, 7122, 7124,7126, 7128, 7130, 7132, 7134, 7136, 7138, 7140, 7142, 7144, 7146, 7148,7150, 7152, 7154, 7156, 7158, 7160, 7162, 7164, 7166, 7168, 7170, 7172,7174, 7176, 7178, 7180, 7182, 7184, 7186, 7188, 7190, 7192, 7194, 7196,7198, 7200, 7202, 7204, 7206, 7208, 7210, 7212, 7214, 7216, 7218, 7220,7222, 7224, 7226, 7228, 7230, 7232, 7234, 7236, 7238, 7240, 7242, 7244,7246, 7248, 7250, 7252, 7254, 7256, 7258, 7260, 7262, 7264, 7266, 7268,7270, 7272, 7274, 7276, 7278, 7280, 7282, 7284, 7286, 7288, 7290, 7292,7294, 7296, 7298, 7300, 7302, 7304, 7306, 7308, 7310, 7312, 7314, 7316,7318, 7320, 7322, 7324, 7326, 7328, 7330, 7332, 7334 1 81 NUE_OEX_1YJR131W S. cerevisiae  7366* Cytoplasmic 7368, 7370, 7372, 7374, 7376,7378, 7380, 7382, 7384, 7386, 7388, 7390, 7392, 7394, 7396, 7398, 7400,7402, 7404, 7406, 7408, 7410, 7412, 7414, 7416, 7418, 7420, 7422, 7424,7426, 7428, 7430, 7432, 7434, 7436, 7438, 7440, 7442, 7444, 7446, 7448,7450, 7452, 7454, 7456, 7458 1 82 NUE_OEX_1 YJR145C S. cerevisiae  7475Cytoplasmic 7477, 7479, 7481, 7483, 7485, 7487, 7489, 7491, 7493, 7495,7497, 7499, 7501, 7503, 7505, 7507, 7509, 7511, 7513, 7515, 7517, 7519,7521, 7523, 7525, 7527, 7529, 7531, 7533, 7535, 7537, 7539, 7541, 7543,7545, 7547, 7549, 7551, 7553, 7555, 7557 1 83 NUE_OEX_1 YKL084W S.cerevisiae  7602 Cytoplasmic 7604, 7606, 7608, 7610, 7612, 7614, 7616,7618, 7620, 7622, 7624, 7626, 7628, 7630, 7632, 7634, 7636, 7638, 7640,7642, 7644 1 84 NUE_OEX_1 YKL088W S. cerevisiae  7651 Cytoplasmic 7653 185 NUE_OEX_1 YKL100C S. cerevisiae  7661* Cytoplasmic 7663, 7665, 7667 186 NUE_OEX_1 YKL131W S. cerevisiae  7675 Cytoplasmic — 1 87 NUE_OEX_1YKL138C S. cerevisiae  7679 Cytoplasmic 7681, 7683, 7685, 7687, 7689,7691, 7693, 7695, 7697, 7699, 7701, 7703 1 88 NUE_OEX_1 YKL178C S.cerevisiae  7710 Cytoplasmic 7712, 7714, 7716, 7718 1 89 NUE_OEX_1YKL179C S. cerevisiae  7735 Cytoplasmic 7737, 7739, 7741, 7743, 7745,7747, 7749, 7751, 7753, 7755, 7757, 7759, 7761, 7763, 7765, 7767 1 90NUE_OEX_1 YKL193C S. cerevisiae  7778* Cytoplasmic 7780, 7782, 7784,7786, 7788, 7790, 7792, 7794, 7796, 7798, 7800, 7802, 7804, 7806, 7808,7810, 7812 1 91 NUE_OEX_1 YKL216W S. cerevisiae  7829 Cytoplasmic 7831,7833, 7835, 7837, 7839, 7841, 7843, 7845, 7847, 7849, 7851, 7853, 7855,7857, 7859, 7861, 7863, 7865, 7867, 7869, 7871, 7873, 7875, 7877, 7879,7881, 7883, 7885, 7887, 7889, 7891, 7893, 7895, 7897, 7899, 7901, 7903,7905, 7907, 7909, 7911, 7913, 7915, 7917, 7919, 7921, 7923, 7925, 7927,7929, 7931, 7933, 7935, 7937, 7939, 7941, 7943, 7945, 7947, 7949, 7951,7953, 7955, 7957, 7959, 7961, 7963, 7965, 7967, 7969, 7971, 7973, 7975,7977, 7979, 7981, 7983, 7985, 7987, 7989, 7991, 7993, 7995, 7997, 7999,8001, 8003, 8005, 8007, 8009, 8011 1 92 NUE_OEX_1 YKR016W S. cerevisiae 8017 Cytoplasmic 8019, 8021, 8023, 8025, 8027, 8029, 8031, 8033, 8035,8037 1 93 NUE_OEX_1 YKR021W S. cerevisiae  8045 Cytoplasmic 8047, 8049,8051, 8053, 8055, 8057, 8059 1 94 NUE_OEX_1 YKR055W S. cerevisiae  8073Cytoplasmic 8075, 8077, 8079, 8081, 8083, 8085, 8087, 8089, 8091, 8093,8095, 8097, 8099, 8101, 8103, 8105, 8107, 8109, 8111, 8113, 8115, 8117,8119, 8121, 8123, 8125, 8127, 8129, 8131, 8133, 8135, 8137, 8139, 8141,8143, 8145, 8147, 8149, 8151, 8153, 8155, 8157, 8159, 8161, 8163, 8165,8167, 8169, 8171, 8173, 8175, 8177, 8179, 8181, 8183, 8185, 8187, 8189,8191, 8193, 8195, 8197, 8199, 8201, 8203, 8205, 8207, 8209, 8211, 8213,8215, 8217, 8219, 8221, 8223, 8225, 8227, 8229, 8231, 8233, 8235, 8237,8239, 8241, 8243, 8245, 8247, 8249, 8251, 8253, 8255 1 95 NUE_OEX_1YKR088C S. cerevisiae  8263 Plastidic 8265, 8267, 8269, 8271, 8273,8275, 8277, 8279 1 96 NUE_OEX_1 YKR093W S. cerevisiae  8287 Cytoplasmic8289, 8291, 8293, 8295, 8297, 8299, 8301, 8303, 8305, 8307, 8309, 8311,8313, 8315, 8317, 8319, 8321, 8323, 8325, 8327, 8329, 8331, 8333, 8335,8337, 8339, 8341, 8343, 8345, 8347, 8349, 8351, 8353, 8355, 8357, 8359,8361, 8363, 8365, 8367, 8369, 8371, 8373, 8375, 8377, 8379, 8381, 8383,8385, 8387, 8389, 8391, 8393, 8395, 8397, 8399, 8401, 8403, 8405, 8407,8409, 8411, 8413, 8415, 8417, 8419, 8421, 8423, 8425, 8427, 8429, 8431,8433, 8435, 8437, 8439, 8441 1 97 NUE_OEX_1 YKR099W S. cerevisiae  8468Cytoplasmic 8470, 8472 1 98 NUE_OEX_1 YKR100C S. cerevisiae  8484Cytoplasmic 8486, 8488 1 99 NUE_OEX_1 YLL014W S. cerevisiae  8492Cytoplasmic 8494, 8496, 8498, 8500, 8502, 8504, 8506, 8508 1 100NUE_OEX_1 YLL016W S. cerevisiae  8514* Cytoplasmic 8516, 8518, 8520,8522, 8524, 8526 1 101 NUE_OEX_1 YLL023C S. cerevisiae  8539 Cytoplasmic8541, 8543, 8545, 8547, 8549, 8551, 8553, 8555, 8557, 8559, 8561, 8563,8565 1 102 NUE_OEX_1 YLL037W S. cerevisiae  8571 Cytoplasmic — 1 103NUE_OEX_1 YLL049W S. cerevisiae  8575 Cytoplasmic — 1 104 NUE_OEX_1YLL055W S. cerevisiae  8579 Cytoplasmic 8581, 8583, 8585, 8587, 8589,8591, 8593, 8595, 8597, 8599, 8601, 8603, 8605, 8607, 8609, 8611, 8613,8615, 8617, 8619, 8621, 8623, 8625, 8627, 8629, 8631, 8633, 8635, 8637,8639, 8641, 8643, 8645, 8647, 8649, 8651, 8653, 8655 1 105 NUE_OEX_1YLR034C S. cerevisiae  8661* Cytoplasmic 8663, 8665, 8667, 8669, 8671,8673, 8675, 8677, 8679, 8681, 8683, 8685, 8687, 8689, 8691, 8693, 8695,8697, 8699, 8701, 8703, 8705, 8707, 8709, 8711, 8713, 8715, 8717, 8719,8721, 8723, 8725, 8727, 8729, 8731, 8733, 8735, 8737, 8739, 8741, 8743,8745, 8747, 8749, 8751, 8753, 8755, 8757, 8759, 8761, 8763, 8765, 8767,8769, 8771, 8773, 8775, 8777, 8779, 8781, 8783, 8785, 8787, 8789, 8791,8793, 8795, 8797, 8799, 8801, 8803, 8805, 8807, 8809, 8811, 8813, 8815,8817, 8819, 8821, 8823, 8825, 8827, 8829, 8831, 8833, 8835, 8837, 8839,8841, 8843, 8845, 8847, 8849, 8851, 8853, 8855, 8857, 8859, 8861, 8863,8865, 8867, 8869, 8871, 8873, 8875, 8877, 8879, 8881, 8883, 8885, 8887,8889, 8891, 8893, 8895, 8897, 8899, 8901, 8903, 8905, 8907, 8909, 8911,8913, 8915, 8917, 8919, 8921, 8923, 8925, 8927, 8929, 8931, 8933, 8935,8937, 8939, 8941, 8943, 8945, 8947, 8949, 8951, 8953, 8955, 8957, 8959,8961 1 106 NUE_OEX_1 YLR042C S. cerevisiae  8991 Cytoplasmic — 1 107NUE_OEX_1 YLR053C S. cerevisiae  8995 Cytoplasmic — 1 108 NUE_OEX_1YLR058C S. cerevisiae  8999 Cytoplasmic 9001, 9003, 9005, 9007, 9009,9011, 9013, 9015, 9017, 9019, 9021, 9023, 9025, 9027, 9029, 9031, 9033,9035, 9037, 9039, 9041, 9043, 9045, 9047, 9049, 9051, 9053, 9055, 9057,9059, 9061, 9063, 9065, 9067, 9069, 9071, 9073, 9075, 9077, 9079, 9081,9083, 9085, 9087, 9089, 9091, 9093, 9095, 9097, 9099, 9101, 9103, 9105,9107, 9109, 9111, 9113, 9115, 9117, 9119, 9121, 9123, 9125, 9127, 9129,9131, 9133, 9135, 9137, 9139, 9141, 9143, 9145, 9147, 9149, 9151, 9153,9155, 9157, 9159, 9161, 9163, 9165, 9167, 9169, 9171, 9173, 9175, 9177,9179, 9181, 9183, 9185, 9187, 9189, 9191, 9193, 9195, 9197, 9199, 9201,9203, 9205, 9207, 9209, 9211, 9213, 9215, 9217, 9219, 9221, 9223, 9225,9227, 9229, 9231, 9233, 9235, 9237, 9239, 9241, 9243, 9245, 9247, 9249,9251, 9253, 9255, 9257, 9259, 9261, 9263, 9265, 9267, 9269, 9271, 9273,9275, 9277, 9279, 9281, 9283, 9285, 9287, 9289, 9291, 9293, 9295, 9297,9299, 9301, 9303, 9305, 9307, 9309, 9311, 9313, 9315, 9317, 9319, 9321,9323, 9325, 9327, 9329, 9331, 9333, 9335, 9337, 9339, 9341, 9343, 9345,9347, 9349, 9351, 9353, 9355, 9357, 9359, 9361, 9363, 9365, 9367, 9369,9371, 9373, 9375, 9377, 9379, 9381, 9383, 9385, 9387, 9389, 9391, 9393,9395, 9397, 9399, 9401, 9403, 9405, 9407, 9409, 9411, 9413, 9415, 9417,9419, 9421, 9423, 9425, 9427, 9429, 9431, 9433, 9435, 9437, 9439, 9441,9443, 9445, 9447, 9449, 9451, 9453, 9455, 9457, 9459, 9461, 9463, 9465,9467, 9469, 9471, 9473, 9475, 9477, 9479, 9481, 9483, 9485, 9487, 9489,9491, 9493, 9495, 9497, 9499 1 109 NUE_OEX_1 YLR060W S. cerevisiae 9551* Cytoplasmic 9553, 9555, 9557, 9559, 9561, 9563, 9565, 9567, 9569,9571, 9573, 9575, 9577, 9579, 9581, 9583, 9585, 9587, 9589, 9591, 9593,9595, 9597, 9599, 9601, 9603, 9605, 9607, 9609, 9611, 9613, 9615, 9617,9619, 9621, 9623, 9625, 9627 1 110 NUE_OEX_1 YLR065C S. cerevisiae  9637Cytoplasmic 9639, 9641, 9643, 9645, 9647, 9649, 9651, 9653, 9655, 9657,9659, 9661, 9663, 9665, 9667 1 111 NUE_OEX_1 YLR070C S. cerevisiae  9672Cytoplasmic 9674, 9676, 9678, 9680, 9682, 9684, 9686, 9688, 9690, 9692,9694, 9696, 9698, 9700, 9702, 9704, 9706, 9708, 9710, 9712, 9714, 9716,9718, 9720, 9722, 9724, 9726, 9728, 9730, 9732, 9734, 9736, 9738, 9740,9742, 9744, 9746, 9748, 9750, 9752, 9754, 9756, 9758, 9760, 9762, 9764,9766, 9768, 9770, 9772, 9774, 9776, 9778, 9780, 9782, 9784, 9786, 9788,9790, 9792, 9794, 9796, 9798, 9800, 9802, 9804, 9806, 9808, 9810, 9812,9814, 9816, 9818, 9820, 9822, 9824, 9826, 9828, 9830, 9832, 9834, 9836,9838, 9840, 9842, 9844, 9846, 9848, 9850, 9852, 9854, 9856, 9858, 9860,9862, 9864, 9866, 9868, 9870, 9872, 9874, 9876, 9878, 9880, 9882, 9884,9886, 9888, 9890, 9892, 9894, 9896, 9898, 9900, 9902, 9904, 9906, 9908,9910, 9912, 9914, 9916, 9918, 9920, 9922, 9924, 9926, 9928, 9930, 9932,9934, 9936, 9938, 9940, 9942, 9944, 9946, 9948, 9950, 9952, 9954, 9956,9958, 9960, 9962, 9964, 9966, 9968, 9970, 9972, 9974, 9976, 9978, 9980,9982, 9984, 9986, 9988, 9990, 9992, 9994, 9996, 9998, 10000, 10002,10004, 10006, 10008, 10010, 10012, 10014, 10016, 10018, 10020, 10022,10024, 10026, 10028, 10030, 10032, 10034, 10036, 10038, 10040, 10042,10044, 10046, 10048, 10050, 10052, 10054, 10056, 10058, 10060, 10062,10064, 10066, 10068, 10070, 10072, 10074, 10076, 10078, 10080, 10082,10084, 10086, 10088, 10090, 10092, 10094, 10096, 10098, 10100, 10102,10104, 10106, 10108, 10110, 10112, 10114, 10116 1 112 NUE_OEX_1 YLR100WS. cerevisiae 10182 Cytoplasmic 10184, 10186, 10188, 10190, 10192,10194, 10196, 10198, 10200, 10202 1 113 NUE_OEX_1 YLR109W S. cerevisiae10214 Cytoplasmic 10216, 10218, 10220, 10222, 10224, 10226, 10228,10230, 10232, 10234, 10236, 10238, 10240, 10242, 10244, 10246, 10248,10250, 10252, 10254, 10256, 10258, 10260, 10262, 10264, 10266, 10268,10270, 10272, 10274, 10276, 10278, 10280, 10282, 10284, 10286, 10288,10290, 10292, 10294, 10296, 10298, 10300, 10302, 10304, 10306, 10308,10310, 10312, 10314, 10316, 10318, 10320, 10322, 10324, 10326, 10328,10330, 10332, 10334, 10336, 10338, 10340, 10342, 10344, 10346, 10348,10350, 10352, 10354, 10356, 10358, 10360, 10362, 10364, 10366, 10368,10370, 10372, 10374, 10376, 10378, 10380, 10382, 10384, 10386, 10388,10390, 10392, 10394, 10396, 10398, 10400, 10402, 10404, 10406, 10408,10410, 10412, 10414, 10416 1 114 NUE_OEX_1 YLR125W S. cerevisiae 10447Cytoplasmic — 1 115 NUE_OEX_1 YLR127C S. cerevisiae 10451 Cytoplasmic10453, 10455, 10457, 10459 1 116 NUE_OEX_1 YLR185W S. cerevisiae 10463Cytoplasmic 10465, 10467, 10469, 10471, 10473, 10475, 10477, 10479,10481, 10483, 10485, 10487, 10489, 10491, 10493, 10495, 10497, 10499,10501, 10503, 10505, 10507, 10509, 10511 1 117 NUE_OEX_1 YLR204W S.cerevisiae 10533 Cytoplasmic 10535, 10537 1 117 NUE_OEX_1 YLR204W S.cerevisiae 10533 Plastidic 10535, 10537 1 118 NUE_OEX_1 YLR242C S.cerevisiae 10541 Cytoplasmic 10543, 10545, 10547, 10549, 10551, 10553 1119 NUE_OEX_1 YLR293C S. cerevisiae 10562 Cytoplasmic 10564, 10566,10568, 10570, 10572, 10574, 10576, 10578, 10580, 10582, 10584, 10586,10588, 10590, 10592, 10594, 10596, 10598, 10600, 10602, 10604, 10606,10608, 10610, 10612, 10614, 10616, 10618, 10620, 10622, 10624, 10626,10628, 10630, 10632, 10634, 10636, 10638, 10640, 10642, 10644, 10646,10648, 10650, 10652, 10654, 10656, 10658, 10660, 10662, 10664, 10666,10668, 10670, 10672, 10674, 10676, 10678, 10680, 10682, 10684, 10686,10688, 10690, 10692, 10694, 10696, 10698, 10700, 10702, 10704, 10706,10708, 10710, 10712 1 120 NUE_OEX_1 YLR313C S. cerevisiae 10990Cytoplasmic 10992, 10994 1 121 NUE_OEX_1 YLR315W S. cerevisiae 10998Cytoplasmic 11000 1 122 NUE_OEX_1 YLR329W S. cerevisiae 11004Cytoplasmic 11006, 11008 1 123 NUE_OEX_1 YLR362W S. cerevisiae 11012Cytoplasmic 11014, 11016, 11018, 11020, 11022, 11024, 11026, 11028,11030, 11032, 11034, 11036, 11038, 11040, 11042 1 124 NUE_OEX_1 YLR395CS. cerevisiae 11054 Cytoplasmic 11056, 11058, 11060 1 125 NUE_OEX_1YLR404W S. cerevisiae 11066 Cytoplasmic 11068, 11070 1 126 NUE_OEX_1YLR463C S. cerevisiae 11074 Cytoplasmic 11076 1 127 NUE_OEX_1 YML022W S.cerevisiae 11080 Cytoplasmic 11082, 11084, 11086, 11088, 11090, 11092,11094, 11096, 11098, 11100, 11102, 11104, 11106, 11108, 11110, 11112,11114, 11116, 11118, 11120, 11122, 11124, 11126, 11128, 11130, 11132,11134, 11136, 11138, 11140, 11142, 11144, 11146, 11148, 11150, 11152,11154, 11156, 11158, 11160, 11162, 11164, 11166, 11168, 11170, 11172,11174, 11176, 11178, 11180, 11182, 11184, 11186, 11188, 11190, 11192,11194, 11196, 11198, 11200, 11202, 11204, 11206, 11208, 11210, 11212,11214, 11216, 11218, 11220, 11222, 11224, 11226, 11228, 11230, 11232,11234, 11236, 11238, 11240, 11242, 11244, 11246, 11248, 11250, 11252,11254, 11256, 11258, 11260, 11262, 11264, 11266, 11268, 11270, 11272,11274, 11276, 11278, 11280, 11282, 11284, 11286, 11288, 11290, 11292,11294, 11296, 11298, 11300, 11302, 11304, 11306, 11308, 11310, 11312,11314, 11316, 11318, 11320, 11322, 11324, 11326, 11328, 11330, 11332,11334, 11336, 11338, 11340, 11342, 11344, 11346, 11348, 11350, 11352,11354, 11356, 11358, 11360, 11362, 11364, 11366, 11368, 11370, 11372,11374, 11376, 11378, 11380, 11382, 11384, 11386, 11388, 11390, 11392,11394, 11396, 11398, 11400, 11402, 11404, 11406, 11408, 11410, 11412,11414, 11416, 11418, 11420, 11422, 11424, 11426, 11428, 11430, 11432,11434, 11436, 11438, 11440, 11442, 11444, 11446, 11448, 11450, 11452,11454, 11456, 11458, 11460, 11462, 11464, 11466, 11468, 11470, 11472,11474, 11476, 11478, 11480, 11482, 11484, 11486, 11488, 11490, 11492,11494, 11496, 11498, 11500, 11502, 11504, 11506, 11508, 11510, 11512,11514, 11516, 11518, 11520, 11522, 11524 1 128 NUE_OEX_1 YML027W S.cerevisiae 11552 Cytoplasmic 11554, 11556, 11558, 11560, 11562 1 129NUE_OEX_1 YML065W S. cerevisiae 11569 Cytoplasmic 11571, 11573, 11575,11577, 11579, 11581, 11583, 11585 1 130 NUE_OEX_1 YML089C S. cerevisiae11596 Cytoplasmic — 1 131 NUE_OEX_1 YML128C S. cerevisiae 11600Cytoplasmic 11602, 11604, 11606, 11608 1 132 NUE_OEX_1 YMR011W S.cerevisiae 11612 Cytoplasmic 11614, 11616, 11618, 11620, 11622, 11624,11626, 11628, 11630, 11632, 11634, 11636, 11638, 11640, 11642, 11644,11646, 11648, 11650, 11652, 11654, 11656, 11658, 11660, 11662, 11664,11666, 11668, 11670, 11672, 11674, 11676, 11678, 11680, 11682, 11684,11686, 11688, 11690, 11692, 11694, 11696, 11698, 11700, 11702, 11704,11706, 11708, 11710, 11712, 11714, 11716, 11718, 11720, 11722, 11724,11726, 11728, 11730, 11732, 11734, 11736, 11738, 11740, 11742, 11744,11746, 11748, 11750, 11752, 11754, 11756, 11758, 11760, 11762, 11764,11766, 11768, 11770, 11772, 11774, 11776, 11778, 11780, 11782, 11784,11786, 11788, 11790, 11792, 11794, 11796, 11798, 11800, 11802, 11804,11806, 11808, 11810, 11812, 11814, 11816, 11818, 11820, 11822, 11824,11826, 11828, 11830, 11832, 11834, 11836, 11838, 11840, 11842, 11844,11846, 11848, 11850, 11852, 11854, 11856, 11858, 11860, 11862, 11864,11866, 11868, 11870, 11872, 11874, 11876, 11878, 11880, 11882, 11884,11886, 11888, 11890, 11892, 11894, 11896, 11898, 11900, 11902, 11904,11906, 11908, 11910, 11912, 11914, 11916, 11918, 11920, 11922, 11924,11926, 11928, 11930, 11932, 11934, 11936, 11938, 11940, 11942, 11944,11946, 11948, 11950, 11952, 11954, 11956, 11958, 11960, 11962, 11964,11966, 11968, 11970, 11972, 11974, 11976, 11978, 11980, 11982, 11984,11986, 11988, 11990, 11992, 11994, 11996, 11998, 12000, 12002, 12004,12006, 12008, 12010, 12012, 12014, 12016, 12018, 12020, 12022, 12024,12026, 12028, 12030, 12032, 12034, 12036, 12038, 12040, 12042, 12044,12046, 12048, 12050, 12052, 12054, 12056, 12058, 12060, 12062, 12064,12066, 12068, 12070, 12072, 12074, 12076, 12078, 12080, 12082, 12084,12086, 12088, 12090, 12092, 12094, 12096, 12098, 12100, 12102, 12104,12106, 12108, 12110, 12112, 12114, 12116, 12118, 12120, 12122 1 133NUE_OEX_1 YMR037C S. cerevisiae 12246 Cytoplasmic 12248, 12250, 12252,12254 1 134 NUE_OEX_1 YMR049C S. cerevisiae 12263 Cytoplasmic 12265,12267, 12269, 12271, 12273, 12275, 12277, 12279, 12281, 12283, 12285,12287, 12289, 12291, 12293, 12295, 12297 1 135 NUE_OEX_1 YMR052W S.cerevisiae 12316 Cytoplasmic 12318, 12320 1 136 NUE_OEX_1 YMR082C S.cerevisiae 12327* Cytoplasmic — 1 137 NUE_OEX_1 YMR125W S. cerevisiae12331 Cytoplasmic 12333, 12335, 12337, 12339, 12341, 12343, 12345,12347, 12349, 12351, 12353, 12355, 12357, 12359, 12361, 12363, 12365 1138 NUE_OEX_1 YMR126C S. cerevisiae 12378 Cytoplasmic 12380, 12382,12384 1 139 NUE_OEX_1 YMR144W S. cerevisiae 12394 Cytoplasmic 12396,12398 1 140 NUE_OEX_1 YMR160W S. cerevisiae 12406 Cytoplasmic 12408,12410 1 141 NUE_OEX_1 YMR191W S. cerevisiae 12414 Cytoplasmic 12416 1142 NUE_OEX_1 YMR209C S. cerevisiae 12420 Cytoplasmic 12422, 12424,12426, 12428 1 143 NUE_OEX_1 YMR233W S. cerevisiae 12440 Cytoplasmic12442, 12444, 12446, 12448, 12450, 12452, 12454, 12456, 12458, 12460,12462, 12464 1 144 NUE_OEX_1 YMR278W S. cerevisiae 12470 Cytoplasmic12472, 12474, 12476, 12478, 12480, 12482, 12484, 12486, 12488, 12490,12492, 12494, 12496, 12498, 12500, 12502, 12504, 12506, 12508, 12510,12512, 12514, 12516, 12518, 12520, 12522, 12524, 12526, 12528, 12530,12532, 12534, 12536, 12538, 12540, 12542, 12544, 12546, 12548, 12550,12552, 12554, 12556, 12558, 12560, 12562, 12564, 12566, 12568, 12570,12572, 12574, 12576, 12578, 12580, 12582, 12584, 12586, 12588, 12590,12592, 12594, 12596, 12598, 12600, 12602, 12604, 12606, 12608, 12610,12612, 12614, 12616, 12618, 12620, 12622, 12624, 12626, 12628, 12630,12632, 12634, 12636, 12638, 12640, 12642, 12644, 12646, 12648, 12650,12652, 12654, 12656, 12658, 12660, 12662, 12664, 12666, 12668, 12670,12672, 12674, 12676, 12678, 12680, 12682, 12684, 12686, 12688, 12690,12692, 12694, 12696, 12698, 12700, 12702, 12704, 12706, 12708, 12710,12712, 12714, 12716, 12718, 12720, 12722, 12724, 12726, 12728, 12730,12732, 12734, 12736, 12738 1 145 NUE_OEX_1 YMR280C S. cerevisiae 12749Cytoplasmic 12751, 12753, 12755 1 146 NUE_OEX_1 YNL014W S. cerevisiae12773 Cytoplasmic 12775, 12777, 12779, 12781, 12783, 12785, 12787,12789, 12791, 12793, 12795, 12797, 12799, 12801, 12803, 12805, 12807,12809 1 147 NUE_OEX_1 YNL320W S. cerevisiae 12829 Cytoplasmic 12831,12833, 12835, 12837, 12839, 12841, 12843, 12845, 12847, 12849, 12851,12853, 12855, 12857, 12859, 12861, 12863, 12865 1 148 NUE_OEX_1 YOL007CS. cerevisiae 12883 Cytoplasmic 12885 1 149 NUE_OEX_1 YOL164W S.cerevisiae 12889 Cytoplasmic 12891, 12893, 12895, 12897, 12899, 12901,12903, 12905, 12907, 12909, 12911, 12913, 12915, 12917, 12919, 12921,12923, 12925, 12927, 12929, 12931, 12933, 12935, 12937, 12939, 12941,12943, 12945, 12947, 12949, 12951, 12953, 12955, 12957, 12959, 12961,12963, 12965, 12967, 12969, 12971, 12973, 12975, 12977, 12979, 12981,12983, 12985, 12987, 12989, 12991, 12993, 12995, 12997, 12999 1 150NUE_OEX_1 YOR076C S. cerevisiae 13014 Cytoplasmic — 1 151 NUE_OEX_1YOR083W S. cerevisiae 13018 Cytoplasmic 13020 1 152 NUE_OEX_1 YOR097C S.cerevisiae 13024 Cytoplasmic 13026 1 153 NUE_OEX_1 YOR128C S. cerevisiae13030 Cytoplasmic 13032, 13034, 13036, 13038, 13040, 13042, 13044,13046, 13048, 13050, 13052, 13054, 13056, 13058, 13060, 13062, 13064,13066, 13068, 13070, 13072, 13074, 13076, 13078, 13080, 13082, 13084,13086, 13088, 13090, 13092, 13094, 13096 1 154 NUE_OEX_1 YOR353C S.cerevisiae 14085 Cytoplasmic 14087, 14089 1 155 NUE_OEX_1 YPL141C S.cerevisiae 14093 Cytoplasmic 14095, 14097, 14099 1 156 NUE_OEX_1 YPR088CS. cerevisiae 14113 Cytoplasmic 14115, 14117, 14119, 14121, 14123,14125, 14127, 14129, 14131, 14133, 14135, 14137, 14139, 14141, 14143,14145, 14147, 14149, 14151, 14153, 14155, 14157, 14159, 14161, 14163,14165, 14167, 14169, 14171, 14173, 14175, 14177, 14179, 14181, 14183,14185, 14187, 14189, 14191, 14193, 14195, 14197, 14199, 14201, 14203,14205, 14207, 14209, 14211, 14213 1 157 NUE_OEX_1 YPR108W S. cerevisiae14246 Cytoplasmic 14248, 14250, 14252, 14254, 14256, 14258, 14260,14262, 14264, 14266, 14268, 14270, 14272, 14274, 14276, 14278, 14280,14282, 14284, 14286, 14288 1 158 NUE_OEX_1 YPR110C S. cerevisiae 14311Cytoplasmic 14313, 14315, 14317, 14319, 14321, 14323, 14325, 14327,14329, 14331, 14333, 14335, 14337, 14339, 14341, 14343, 14345, 14347,14349, 14351, 14353, 14355, 14357, 14359, 14361, 14363, 14365, 14367,14369, 14371 1 159 NUE_OEX_1 B3825_2 E. coli 14914 Plastidic 14916,14918, 14920, 14922, 14924, 14926, 14928, 14930, 14932, 14934, 14936,14938, 14940, 14942, 14944, 14946, 14948, 14950, 14952, 14954, 14956,14958, 14960, 14962, 14964, 14966, 14968, 14970, 14972, 14974, 14976,14978, 14980, 14982, 14984, 14986, 14988, 14990, 14992, 14994, 14996,14998, 15000, 15002, 15004, 15006, 15008 1 160 NUE_OEX_1 YIR034C_2 S.cerevisiae 15382 Cytoplasmic 15384, 15386, 15388, 15390, 15392, 15394,15396, 15398, 15400, 15402, 15404, 15406, 15408, 15410, 15412, 15414,15416, 15418 1 161 NUE_OEX_1 YJR131W_2 S. cerevisiae 15460 Cytoplasmic15462, 15464, 15466, 15468, 15470, 15472, 15474, 15476, 15478, 15480,15482, 15484, 15486, 15488, 15490, 15492, 15494, 15496, 15498, 15500,15502, 15504, 15506, 15508, 15510, 15512, 15514, 15516, 15518, 15520,15522, 15524, 15526, 15528, 15530, 15532, 15534, 15536, 15538, 15540,15542, 15544, 15546, 15548, 15550, 15552, 15554 1 162 NUE_OEX_1YKL100C_2 S. cerevisiae 15571 Cytoplasmic 15573, 15575, 15577, 15579 1163 NUE_OEX_1 YKL193C_2 S. cerevisiae 15593 Cytoplasmic 15595, 15597,15599, 15601, 15603, 15605, 15607, 15609, 15611, 15613, 15615, 15617,15619, 15621, 15623, 15625, 15627, 15629 1 164 NUE_OEX_1 YLL016W_2 S.cerevisiae 15646 Cytoplasmic 15648, 15650, 15652, 15654, 15656, 15658,15660 1 165 NUE_OEX_1 YLR034C_2 S. cerevisiae 15673 Cytoplasmic 15675,15677, 15679, 15681, 15683, 15685, 15687, 15689, 15691, 15693, 15695,15697, 15699, 15701, 15703, 15705, 15707, 15709, 15711, 15713, 15715,15717, 15719, 15721, 15723, 15725, 15727, 15729, 15731, 15733, 15735,15737, 15739, 15741, 15743, 15745, 15747, 15749, 15751, 15753, 15755,15757, 15759, 15761, 15763, 15765, 15767, 15769, 15771, 15773, 15775,15777, 15779, 15781, 15783, 15785, 15787, 15789, 15791, 15793, 15795,15797, 15799, 15801, 15803, 15805, 15807, 15809, 15811, 15813, 15815,15817, 15819, 15821, 15823, 15825, 15827, 15829, 15831, 15833, 15835,15837, 15839, 15841, 15843, 15845, 15847, 15849, 15851, 15853, 15855,15857, 15859, 15861, 15863, 15865, 15867, 15869, 15871, 15873, 15875,15877, 15879, 15881, 15883, 15885, 15887, 15889, 15891, 15893, 15895,15897, 15899, 15901, 15903, 15905, 15907, 15909, 15911, 15913, 15915,15917, 15919, 15921, 15923, 15925, 15927, 15929, 15931, 15933, 15935,15937, 15939, 15941, 15943, 15945, 15947, 15949, 15951, 15953, 15955,15957, 15959, 15961, 15963, 15965, 15967, 15969, 15971, 15973, 15975 1166 NUE_OEX_1 YLR060W_2 S. cerevisiae 16005 Cytoplasmic 16007, 16009,16011, 16013, 16015, 16017, 16019, 16021, 16023, 16025, 16027, 16029,16031, 16033, 16035, 16037, 16039, 16041, 16043, 16045, 16047, 16049,16051, 16053, 16055, 16057, 16059, 16061, 16063, 16065, 16067, 16069,16071, 16073, 16075, 16077, 16079, 16081, 16083 1 167 NUE_OEX_1YMR082C_2 S. cerevisiae 16114 Cytoplasmic 16116 1 168 NUE_OEX_1 B1258 E.coli 14402 Cytoplasmic 14404, 14406, 14408, 14410, 14412, 14414, 14416,14418, 14420, 14422, 14424, 14426, 14428, 14430, 14432, 14434, 14436,14438, 14440, 14442, 14444, 14446, 14448, 14450, 14452, 14454, 14456,14458, 14460, 14462, 14464, 14466, 14468, 14470, 14472, 14474, 14476,14478, 14480, 14482, 14484, 14486, 14488, 14490 1 169 NUE_OEX_1 YML101CS. cerevisiae 16093 Cytoplasmic 16095, 16097, 16099 1 170 NUE_OEX_1YMR065W S. cerevisiae 16106 Cytoplasmic 16108, 16110 1 171 NUE_OEX_1YMR163C S. cerevisiae 16120 Cytoplasmic 16122, 16124, 16126 1 172NUE_OEX_1 YOL042W S. cerevisiae 16275 Cytoplasmic 16277, 16279, 16281,16283, 16285, 16287 1 173 NUE_OEX_1 YOR226C S. cerevisiae 16305Cytoplasmic 16307, 16309, 16311, 16313, 16315, 16317, 16319, 16321,16323, 16325, 16327, 16329, 16331, 16333, 16335, 16337, 16339, 16341,16343, 16345, 16347, 16349, 16351, 16353, 16355, 16357, 16359, 16361,16363, 16365, 16367, 16369, 16371, 16373, 16375, 16377, 16379, 16381,16383, 16385, 16387, 16389, 16391, 16393, 16395, 16397, 16399, 16401,16403, 16405, 16407, 16409, 16411, 16413, 16415, 16417, 16419, 16421,16423, 16425, 16427, 16429, 16431, 16433, 16435, 16437, 16439, 16441,16443, 16445, 16447, 16449, 16451, 16453, 16455, 16457, 16459, 16461,16463, 16465, 16467, 16469, 16471, 16473, 16475, 16477, 16479, 16481,16483, 16485, 16487, 16489, 16491, 16493, 16495, 16497, 16499, 16501,16503, 16505, 16507, 16509, 16511, 16513, 16515, 16517, 16519, 16521,16523, 16525, 16527, 16529, 16531, 16533, 16535 1 174 NUE_OEX_1 YPL068CS. cerevisiae 16573 Cytoplasmic 16575, 16577 1 175 NUE_OEX_1 B0165 E.coli 14396 Plastidic 14398 1 176 NUE_OEX_1 YOR203W S. cerevisiae 16299Cytoplasmic 16301 1 177 NUE_OEX_1 YNL147W S. cerevisiae 16133Cytoplasmic 16135, 16137, 16139, 16141, 16143, 16145, 16147, 16149,16151, 16153, 16155, 16157, 16159, 16161, 16163, 16165, 16167, 16169,16171, 16173, 16175, 16177, 16179, 16181, 16183, 16185, 16187, 16189,16191, 16193, 16195, 16197, 16199, 16201, 16203, 16205, 16207, 16209,16211, 16213, 16215, 16217, 16219, 16221, 16223, 16225, 16227, 16229,16231, 16233, 16235, 16237, 16239, 16241, 16243, 16245, 16247, 16249,16251, 16253, 16255 1 178 NUE_OEX_1 YBR083W S. cerevisiae 15056Cytoplasmic 15058, 15060 1 179 NUE_OEX_1 YKL111C S. cerevisiae 15587Cytoplasmic 15589 1 180 NUE_OEX_1 YPR067W S. cerevisiae 16582Cytoplasmic 16584, 16586, 16588, 16590, 16592, 16594, 16596, 16598,16600, 16602, 16604, 16606, 16608, 16610, 16612, 16614, 16616, 16618,16620, 16622 1 181 NUE_OEX_1 B1985 E. coli 14839 Cytoplasmic 14841,14843, 14845, 14847, 14849, 14851, 14853, 14855, 14857, 14859, 14861,14863, 14865 1 182 NUE_OEX_1 B3838 E. coli 15014 Cytoplasmic 15016,15018, 15020, 15022, 15024, 15026, 15028, 15030, 15032, 15034, 15036,15038, 15040, 15042, 15044, 15046, 15048 1 183 NUE_OEX_1 YJL010C S.cerevisiae 15432 Cytoplasmic 15434, 15436, 15438, 15440, 15442, 15444,15446, 15448 1 184 NUE_OEX_1 B1267 E. coli 14497 Cytoplasmic 14499,14501, 14503, 14505, 14507, 14509, 14511, 14513, 14515, 14517, 14519,14521, 14523, 14525, 14527, 14529, 14531, 14533, 14535, 14537, 14539,14541, 14543, 14545, 14547, 14549, 14551, 14553, 14555, 14557, 14559,14561, 14563, 14565, 14567, 14569, 14571, 14573, 14575, 14577, 14579,14581, 14583, 14585, 14587, 14589, 14591, 14593, 14595, 14597, 14599,14601, 14603, 14605, 14607, 14609, 14611, 14613, 14615, 14617, 14619,14621, 14623, 14625, 14627, 14629, 14631, 14633, 14635, 14637, 14639,14641, 14643, 14645, 14647, 14649, 14651, 14653, 14655, 14657, 14659,14661, 14663, 14665, 14667, 14669, 14671, 14673, 14675, 14677, 14679,14681, 14683, 14685, 14687, 14689, 14691, 14693, 14695, 14697, 14699,14701, 14703, 14705, 14707 1 185 NUE_OEX_1 B1322 E. coli 14718Cytoplasmic 14720, 14722, 14724, 14726, 14728, 14730, 14732, 14734,14736, 14738, 14740, 14742, 14744, 14746, 14748, 14750, 14752, 14754,14756, 14758, 14760, 14762, 14764, 14766, 14768, 14770, 14772, 14774,14776, 14778, 14780, 14782, 14784 1 186 NUE_OEX_1 B1381 E. coli 14791Cytoplasmic 14793, 14795, 14797, 14799, 14801, 14803, 14805, 14807,14809, 14811, 14813, 14815, 14817, 14819 1 187 NUE_OEX_1 B2646 E. coli14879 Cytoplasmic 14881, 14883, 14885, 14887, 14889, 14891, 14893,14895, 14897, 14899, 14901, 14903, 14905, 14907 1 188 NUE_OEX_1 YBR191WS. cerevisiae 15064 Cytoplasmic 15066, 15068, 15070, 15072, 15074,15076, 15078, 15080, 15082, 15084, 15086, 15088, 15090, 15092, 15094,15096, 15098, 15100, 15102, 15104, 15106, 15108, 15110, 15112, 15114,15116, 15118, 15120, 15122, 15124, 15126, 15128, 15130, 15132, 15134,15136, 15138, 15140, 15142, 15144, 15146, 15148, 15150, 15152, 15154,15156, 15158, 15160, 15162, 15164, 15166, 15168, 15170, 15172, 15174,15176, 15178, 15180, 15182, 15184, 15186, 15188, 15190, 15192, 15194,15196, 15198, 15200, 15202, 15204, 15206, 15208, 15210, 15212, 15214,15216 1 189 NUE_OEX_1 YDL135C S. cerevisiae 15257 Cytoplasmic 15259,15261, 15263, 15265, 15267, 15269, 15271, 15273, 15275, 15277, 15279,15281, 15283, 15285, 15287, 15289, 15291, 15293, 15295, 15297, 15299,15301, 15303, 15305, 15307, 15309, 15311, 15313, 15315, 15317, 15319,15321, 15323, 15325, 15327, 15329, 15331, 15333, 15335, 15337, 15339,15341, 15343, 15345, 15347, 15349, 15351, 15353, 15355 1 190 NUE_OEX_1YHL005C S. cerevisiae 15378 Cytoplasmic — 1 191 NUE_OEX_1 YKR100C_2 S.cerevisiae 16629 Cytoplasmic 16631, 16633, 16635, 16637 1 192 NUE_OEX_1YMR191W_2 S. cerevisiae 16647 Cytoplasmic 16649, 16651

TABLE IA _CHOM Nucleic acid sequence ID numbers 5. Appli- 1. 2. 3. 4.Lead 6. 7. cation Hit Project Locus Organism SEQ ID Target SEQ IDs ofNucleic Acid Homologs 1 1 NUE_OEX_1 yor128c S. cerevisiae 13030Cytoplasmic 13117, 13119, 13121, 13123, 13125, 13127, 13129, 13131, CHOM13133, 13135, 13137, 13139, 13141, 13143, 13145, 13147, 13149, 13151,13153, 13155, 13157, 13159, 13161, 13163, 13165, 13167, 13169, 13171,13173, 13175, 13177, 13179, 13181, 13183, 13185, 13187, 13189, 13191,13193, 13195, 13197, 13199, 13201, 13203, 13205, 13207, 13209, 13211,13213, 13215, 13217, 13219, 13221, 13223, 13225, 13227, 13229, 13231,13233, 13235, 13237, 13239, 13241, 13243, 13245, 13247, 13249, 13251,13253, 13255, 13257, 13259, 13261, 13263, 13265, 13267, 13269, 13271,13273, 13275, 13277, 13279, 13281, 13283, 13285, 13287, 13289, 13291,13293, 13295, 13297, 13299, 13301, 13303, 13305, 13307, 13309, 13311,13313, 13315, 13317, 13319, 13321, 13323, 13325, 13327, 13329, 13331,13333, 13335, 13337, 13339, 13341, 13343, 13345, 13347, 13349, 13351,13353, 13355, 13357, 13359, 13361, 13363, 13365, 13367, 13369, 13371,13373, 13375, 13377, 13379, 13381, 13383, 13385, 13387, 13389, 13391,13393, 13395, 13397, 13399, 13401, 13403, 13405, 13407, 13409, 13411,13413, 13415, 13417, 13419, 13421, 13423, 13425, 13427, 13429, 13431,13433, 13435, 13437, 13439, 13441, 13443, 13445, 13447, 13449, 13451,13453, 13455, 13457, 13459, 13461, 13463, 13465, 13467, 13469, 13471,13473, 13475, 13477, 13479, 13481, 13483, 13485, 13487, 13489, 13491,13493, 13495, 13497, 13499, 13501, 13503, 13505, 13507, 13509, 13511,13513, 13515, 13517, 13519, 13521, 13523, 13525, 13527, 13529, 13531,13533, 13535, 13537, 13539, 13541, 13543, 13545, 13547, 13549, 13551,13553, 13555, 13557, 13559, 13561, 13563, 13565, 13567, 13569, 13571,13573, 13575, 13577, 13579, 13581, 13583, 13585, 13587, 13589, 13591,13593, 13595, 13597, 13599, 13601, 13603, 13605, 13607, 13609, 13611,13613, 13615

TABLE IA _NHOM Nucleic acid sequence ID numbers 5. Appli- 1. 2. 3. 4.Lead 6. 7. cation Hit Project Locus Organism SEQ ID Target SEQ IDs ofNucleic Acid Homologs 1 1 NUE_OEX_1 yor128c S. cerevisiae 13030Cytoplasmic 13624, 13626, 13628, 13630, 13632, 13634, 13636, 13638, NHOM13640, 13642, 13644, 13646, 13648, 13650, 13652, 13654, 13656, 13658,13660, 13662, 13664, 13666, 13668, 13670, 13672, 13674, 13676, 13678,13680, 13682, 13684, 13686, 13688, 13690, 13692, 13694, 13696, 13698,13700, 13702, 13704, 13706, 13708, 13710, 13712, 13714, 13716, 13718,13720, 13722, 13724, 13726, 13728, 13730, 13732, 13734, 13736, 13738,13740, 13742, 13744, 13746, 13748, 13750, 13752, 13754, 13756, 13758,13760, 13762, 13764, 13766, 13768, 13770, 13772, 13774, 13776, 13778,13780, 13782, 13784, 13786, 13788, 13790, 13792, 13794, 13796, 13798,13800, 13802, 13804, 13806, 13808, 13810, 13812, 13814, 13816, 13818,13820, 13822, 13824, 13826, 13828, 13830, 13832, 13834, 13836, 13838,13840, 13842, 13844, 13846, 13848, 13850, 13852, 13854, 13856, 13858,13860, 13862, 13864, 13866, 13868, 13870, 13872, 13874, 13876, 13878,13880, 13882, 13884, 13886, 13888, 13890, 13892, 13894, 13896, 13898,13900, 13902, 13904, 13906, 13908, 13910, 13912, 13914, 13916, 13918,13920, 13922, 13924, 13926, 13928, 13930, 13932, 13934, 13936, 13938,13940, 13942, 13944, 13946, 13948, 13950, 13952, 13954, 13956, 13958,13960, 13962, 13964, 13966, 13968, 13970, 13972, 13974, 13976, 13978,13980, 13982, 13984, 13986, 13988, 13990, 13992, 13994, 13996, 13998,14000, 14002, 14004, 14006, 14008, 14010, 14012, 14014, 14016, 14018,14020, 14022, 14024, 14026, 14028, 14030, 14032, 14034, 14036, 14038,14040, 14042, 14044, 14046, 14048, 14050, 14052, 14054, 14056, 14058,14060, 14062, 14064, 14066, 14068, 14070, 14072, 14074, 14076, 14078,14080

TABLE IB Nucleic acid sequence ID numbers Ap- pli- 5. ca- 1. 2. 3. 4.Lead 6. 7. tion Hit Project Locus Organism SEQ ID Target SEQ IDs ofNucleic Acid Homologs 1 1 NUE_OEX_1 B0017 E. coli   38 Cytoplasmic — 1 2NUE_OEX_1 B0045 E. coli   42 Cytoplasmic 98, 100, 102, 104, 106, 108,110, 112, 114, 116 1 3 NUE_OEX_1 B0180 E. coli  123 Plastidic 365, 367,369, 371, 373 1 4 NUE_OEX_1 B0242 E. coli  380 Plastidic 662, 664, 666,668 1 5 NUE_OEX_1 B0403 E. coli  679 Plastidic — 1 6 NUE_OEX_1 B0474 E.coli  812 Cytoplasmic 958, 960, 962, 964, 966, 968, 970, 972, 974, 976,978, 980, 982, 984, 986, 988, 990, 992, 994, 996, 998, 1000, 1002, 1004,1006, 1008, 1010, 1012, 1014, 1016, 1018, 1020, 1022, 1024, 1026, 1028,1030, 1032, 1034, 1036, 1038, 1040, 1042, 1044, 1046, 1048, 16657 1 7NUE_OEX_1 B0754 E. coli  1055 Plastidic — 1 8 NUE_OEX_1 B0784 E. coli 1563 Cytoplasmic — 1 9 NUE_OEX_1 B0873 E. coli  1705 Plastidic — 1 10NUE_OEX_1 B1014 E. coli  1844 Cytoplasmic — 1 11 NUE_OEX_1 B1020 E. coli 1950 Plastidic — 1 12 NUE_OEX_1 B1180 E. coli  1975 Cytoplasmic 2099,2101, 2103, 2105, 2107, 2109, 2111, 2113, 2115, 2117, 2119, 16661 1 13NUE_OEX_1 B1933 E. coli  2127 Plastidic — 1 14 NUE_OEX_1 B2032 E. coli 2135 Plastidic — 1 15 NUE_OEX_1 B2165 E. coli  2171 Plastidic 2285,2287 1 16 NUE_OEX_1 B2223 E. coli  2297 Plastidic — 1 17 NUE_OEX_1 B2238E. coli  2426 Plastidic — 1 17 NUE_OEX_1 B2238 E. coli  2426 Cytoplasmic— 1 18 NUE_OEX_1 B2310 E. coli  2452 Plastidic — 1 19 NUE_OEX_1 B2431 E.coli  2551 Plastidic — 1 20 NUE_OEX_1 B2600 E. coli  2600 Plastidic — 121 NUE_OEX_1 B2766 E. coli  2668 Plastidic — 1 22 NUE_OEX_1 B2903 E.coli  2772 Cytoplasmic 3096, 3098 1 23 NUE_OEX_1 B3117 E. coli  3117Plastidic 3373, 3375, 3377, 3379, 3381 1 24 NUE_OEX_1 B3120 E. coli 3390 Plastidic — 1 25 NUE_OEX_1 B3216 E. coli  3396 Plastidic — 1 26NUE_OEX_1 B3451 E. coli  3470 Plastidic — 1 27 NUE_OEX_1 B3791 E. coli 3563 Cytoplasmic — 1 28 NUE_OEX_1 B3825 E. coli  3770* Plastidic — 1 29NUE_OEX_1 YAL019W S. cerevisiae  3868 Cytoplasmic — 1 30 NUE_OEX_1YAR035W S. cerevisiae  3895 Cytoplasmic — 1 31 NUE_OEX_1 YBL021C S.cerevisiae  3953 Cytoplasmic 4031, 4033, 4035, 4037, 4039, 4041, 4043,4045, 4047, 4049, 4051, 4053, 4055, 4057, 4059, 4061, 4063, 4065, 4067,4069, 4071, 4073, 4075, 4077, 4079, 4081, 4083, 4085, 4087, 4089, 4091,4093, 4095, 4097, 4099, 4101, 4103, 4105 1 32 NUE_OEX_1 YBR055C S.cerevisiae  4111 Cytoplasmic — 1 33 NUE_OEX_1 YBR128C S. cerevisiae 4149 Cytoplasmic — 1 34 NUE_OEX_1 YBR159W S. cerevisiae  4162Cytoplasmic 4214, 4216, 4218, 4220, 4222, 4224, 4226 1 35 NUE_OEX_1YBR243C S. cerevisiae  4235 Cytoplasmic 4267, 4269 1 35 NUE_OEX_1YBR243C S. cerevisiae  4235 Plastidic 4267, 4269 1 36 NUE_OEX_1 YBR262CS. cerevisiae  4280 Cytoplasmic — 1 37 NUE_OEX_1 YCR019W S. cerevisiae 4288 Cytoplasmic — 1 38 NUE_OEX_1 YDR070C S. cerevisiae  4315Cytoplasmic — 1 39 NUE_OEX_1 YDR079W S. cerevisiae  4325 Cytoplasmic — 140 NUE_OEX_1 YDR123C S. cerevisiae  4335 Cytoplasmic — 1 41 NUE_OEX_1YDR137W S. cerevisiae  4346 Cytoplasmic — 1 42 NUE_OEX_1 YDR294C S.cerevisiae  4361 Cytoplasmic — 1 42 NUE_OEX_1 YDR294C S. cerevisiae 4361 Plastidic — 1 43 NUE_OEX_1 YDR330W S. cerevisiae  4402 Cytoplasmic— 1 44 NUE_OEX_1 YDR355C S. cerevisiae  4431 Cytoplasmic — 1 45NUE_OEX_1 YDR430C S. cerevisiae  4435 Plastidic — 1 46 NUE_OEX_1 YDR472WS. cerevisiae  4485 Cytoplasmic — 1 47 NUE_OEX_1 YDR497C S. cerevisiae 4506 Plastidic 4738, 4740, 4742, 4744, 4746, 4748, 4750, 4752, 4754,4756, 4758, 4760, 4762, 4764, 4766, 4768, 4770, 4772, 4774, 4776, 4778,4780, 4782, 4784, 16665 1 48 NUE_OEX_1 YER029C S. cerevisiae  4790Cytoplasmic — 1 49 NUE_OEX_1 YFR007W S. cerevisiae  4806 Cytoplasmic — 150 NUE_OEX_1 YGL039W S. cerevisiae  4836 Cytoplasmic 5214, 5216, 5218,5220, 5222, 5224, 5226, 5228, 5230, 5232, 5234, 5236, 5238, 5240, 5242,5244, 5246, 5248, 5250, 5252, 5254, 5256, 5258, 5260, 5262, 5264, 5266,5268, 5270, 5272, 5274, 5276, 5278, 5280, 5282, 5284, 5286, 5288, 5290,5292, 5294, 5296, 5298, 5300, 5302, 5304 1 51 NUE_OEX_1 YGL043W S.cerevisiae  5311 Cytoplasmic 5335, 5337, 5339 1 52 NUE_OEX_1 YGR088W S.cerevisiae  5346 Cytoplasmic 5524 1 53 NUE_OEX_1 YGR122C-A S. cerevisiae 5533 Cytoplasmic — 1 54 NUE_OEX_1 YGR142W S. cerevisiae  5551Cytoplasmic — 1 55 NUE_OEX_1 YGR143W S. cerevisiae  5559 Cytoplasmic — 156 NUE_OEX_1 YGR165W S. cerevisiae  5602 Cytoplasmic — 1 57 NUE_OEX_1YGR170W S. cerevisiae  5608 Cytoplasmic — 1 58 NUE_OEX_1 YGR202C S.cerevisiae  5614 Cytoplasmic — 1 59 NUE_OEX_1 YGR266W S. cerevisiae 5666 Cytoplasmic — 1 60 NUE_OEX_1 YGR282C S. cerevisiae  5701Cytoplasmic — 1 61 NUE_OEX_1 YGR290W S. cerevisiae  5750 Cytoplasmic — 162 NUE_OEX_1 YHL021C S. cerevisiae  5754 Cytoplasmic — 1 63 NUE_OEX_1YHL031C S. cerevisiae  5778 Cytoplasmic — 1 64 NUE_OEX_1 YHR011W S.cerevisiae  5812 Cytoplasmic 5954, 5956, 5958, 16669 1 65 NUE_OEX_1YHR127W S. cerevisiae  5967 Cytoplasmic — 1 66 NUE_OEX_1 YHR137W S.cerevisiae  5973 Cytoplasmic — 1 66 NUE_OEX_1 YHR137W S. cerevisiae 5973 Plastidic — 1 67 NUE_OEX_1 YIL099W S. cerevisiae  6027 Cytoplasmic— 1 67 NUE_OEX_1 YIL099W S. cerevisiae  6027 Plastidic — 1 68 NUE_OEX_1YIL147C S. cerevisiae  6107 Cytoplasmic — 1 69 NUE_OEX_1 YIR034C S.cerevisiae  6150* Cytoplasmic — 1 70 NUE_OEX_1 YJL013C S. cerevisiae 6198 Cytoplasmic — 1 71 NUE_OEX_1 YJL041W S. cerevisiae  6208Cytoplasmic — 1 72 NUE_OEX_1 YJL064W S. cerevisiae  6242 Cytoplasmic — 173 NUE_OEX_1 YJL067W S. cerevisiae  6246 Cytoplasmic — 1 74 NUE_OEX_1YJL094C S. cerevisiae  6250 Cytoplasmic — 1 75 NUE_OEX_1 YJL171C S.cerevisiae  6297 Cytoplasmic — 1 76 NUE_OEX_1 YJL213W S. cerevisiae 6326 Cytoplasmic — 1 77 NUE_OEX_1 YJR017C S. cerevisiae  6488Cytoplasmic 6542 1 78 NUE_OEX_1 YJR058C S. cerevisiae  6550 Cytoplasmic6662, 6664, 6666, 6668, 6670, 6672, 6674, 6676, 6678, 6680, 6682, 6684,6686, 6688, 6690, 6692, 6694, 16673, 16675 1 79 NUE_OEX_1 YJR117W S.cerevisiae  6700 Cytoplasmic 6790, 6792, 6794, 6796, 6798, 6800, 6802,6804, 6806 1 80 NUE_OEX_1 YJR121W S. cerevisiae  6816 Cytoplasmic 7336,7338, 7340, 7342, 7344, 7346, 7348 1 81 NUE_OEX_1 YJR131W S. cerevisiae 7366* Cytoplasmic 7460, 7462, 7464, 7466 1 82 NUE_OEX_1 YJR145C S.cerevisiae  7475 Cytoplasmic 7559, 7561, 7563, 7565, 7567, 7569, 7571,7573, 7575, 7577, 7579, 7581, 7583, 7585, 7587, 7589, 7591, 7593, 7595,16679 1 83 NUE_OEX_1 YKL084W S. cerevisiae  7602 Cytoplasmic — 1 84NUE_OEX_1 YKL088W S. cerevisiae  7651 Cytoplasmic — 1 85 NUE_OEX_1YKL100C S. cerevisiae  7661* Cytoplasmic — 1 86 NUE_OEX_1 YKL131W S.cerevisiae  7675 Cytoplasmic — 1 87 NUE_OEX_1 YKL138C S. cerevisiae 7679 Cytoplasmic — 1 88 NUE_OEX_1 YKL178C S. cerevisiae  7710Cytoplasmic — 1 89 NUE_OEX_1 YKL179C S. cerevisiae  7735 Cytoplasmic — 190 NUE_OEX_1 YKL193C S. cerevisiae  7778* Cytoplasmic 7814, 7816, 7818,7820 1 91 NUE_OEX_1 YKL216W S. cerevisiae  7829 Cytoplasmic — 1 92NUE_OEX_1 YKR016W S. cerevisiae  8017 Cytoplasmic — 1 93 NUE_OEX_1YKR021W S. cerevisiae  8045 Cytoplasmic — 1 94 NUE_OEX_1 YKR055W S.cerevisiae  8073 Cytoplasmic 8257 1 95 NUE_OEX_1 YKR088C S. cerevisiae 8263 Plastidic — 1 96 NUE_OEX_1 YKR093W S. cerevisiae  8287 Cytoplasmic8443, 8445, 8447, 8449, 8451, 8453, 8455, 8457, 8459, 8461 1 97NUE_OEX_1 YKR099W S. cerevisiae  8468 Cytoplasmic — 1 98 NUE_OEX_1YKR100C S. cerevisiae  8484 Cytoplasmic — 1 99 NUE_OEX_1 YLL014W S.cerevisiae  8492 Cytoplasmic — 1 100 NUE_OEX_1 YLL016W S. cerevisiae 8514* Cytoplasmic — 1 101 NUE_OEX_1 YLL023C S. cerevisiae  8539Cytoplasmic — 1 102 NUE_OEX_1 YLL037W S. cerevisiae  8571 Cytoplasmic —1 103 NUE_OEX_1 YLL049W S. cerevisiae  8575 Cytoplasmic — 1 104NUE_OEX_1 YLL055W S. cerevisiae  8579 Cytoplasmic — 1 105 NUE_OEX_1YLR034C S. cerevisiae  8661* Cytoplasmic 8963, 8965, 8967, 8969, 8971,8973, 8975, 8977, 8979, 8981 1 106 NUE_OEX_1 YLR042C S. cerevisiae  8991Cytoplasmic — 1 107 NUE_OEX_1 YLR053C S. cerevisiae  8995 Cytoplasmic —1 108 NUE_OEX_1 YLR058C S. cerevisiae  8999 Cytoplasmic 9501, 9503,9505, 9507, 9509, 9511, 9513, 9515, 9517, 9519, 9521, 9523, 9525, 9527,9529, 9531, 9533, 9535, 9537, 9539 1 109 NUE_OEX_1 YLR060W S. cerevisiae 9551* Cytoplasmic — 1 110 NUE_OEX_1 YLR065C S. cerevisiae  9637Cytoplasmic — 1 111 NUE_OEX_1 YLR070C S. cerevisiae  9672 Cytoplasmic10118, 10120, 10122, 10124, 10126, 10128, 10130, 10132, 10134, 10136,10138, 10140, 10142, 10144, 10146, 10148, 10150, 10152, 10154, 10156,10158, 10160, 10162, 10164, 10166, 10168, 10170, 10172, 10174, 10176 1112 NUE_OEX_1 YLR100W S. cerevisiae 10182 Cytoplasmic — 1 113 NUE_OEX_1YLR109W S. cerevisiae 10214 Cytoplasmic 10418, 10420, 10422, 10424,10426, 10428, 10430, 10432, 10434, 10436, 10438, 10440, 10442 1 114NUE_OEX_1 YLR125W S. cerevisiae 10447 Cytoplasmic — 1 115 NUE_OEX_1YLR127C S. cerevisiae 10451 Cytoplasmic — 1 116 NUE_OEX_1 YLR185W S.cerevisiae 10463 Cytoplasmic 10513, 10515, 10517, 10519, 10521, 10523,10525 1 117 NUE_OEX_1 YLR204W S. cerevisiae 10533 Cytoplasmic — 1 117NUE_OEX_1 YLR204W S. cerevisiae 10533 Plastidic — 1 118 NUE_OEX_1YLR242C S. cerevisiae 10541 Cytoplasmic — 1 119 NUE_OEX_1 YLR293C S.cerevisiae 10562 Cytoplasmic 10714, 10716, 10718, 10720, 10722, 10724,10726, 10728, 10730, 10732, 10734, 10736, 10738, 10740, 10742, 10744,10746, 10748, 10750, 10752, 10754, 10756, 10758, 10760, 10762, 10764,10766, 10768, 10770, 10772, 10774, 10776, 10778, 10780, 10782, 10784,10786, 10788, 10790, 10792, 10794, 10796, 10798, 10800, 10802, 10804,10806, 10808, 10810, 10812, 10814, 10816, 10818, 10820, 10822, 10824,10826, 10828, 10830, 10832, 10834, 10836, 10838, 10840, 10842, 10844,10846, 10848, 10850, 10852, 10854, 10856, 10858, 10860, 10862, 10864,10866, 10868, 10870, 10872, 10874, 10876, 10878, 10880, 10882, 10884,10886, 10888, 10890, 10892, 10894, 10896, 10898, 10900, 10902, 10904,10906, 10908, 10910, 10912, 10914, 10916, 10918, 10920, 10922, 10924,10926, 10928, 10930, 10932, 10934, 10936, 10938, 10940, 10942, 10944,10946, 10948, 10950, 10952, 10954, 10956, 10958, 10960, 10962, 10964,10966, 10968, 10970, 10972, 10974, 10976, 10978, 10980, 10982 1 120NUE_OEX_1 YLR313C S. cerevisiae 10990 Cytoplasmic — 1 121 NUE_OEX_1YLR315W S. cerevisiae 10998 Cytoplasmic — 1 122 NUE_OEX_1 YLR329W S.cerevisiae 11004 Cytoplasmic — 1 123 NUE_OEX_1 YLR362W S. cerevisiae11012 Cytoplasmic — 1 124 NUE_OEX_1 YLR395C S. cerevisiae 11054Cytoplasmic — 1 125 NUE_OEX_1 YLR404W S. cerevisiae 11066 Cytoplasmic —1 126 NUE_OEX_1 YLR463C S. cerevisiae 11074 Cytoplasmic — 1 127NUE_OEX_1 YML022W S. cerevisiae 11080 Cytoplasmic 11526, 11528, 11530,11532, 11534, 11536, 11538, 11540, 11542, 11544, 11546 1 128 NUE_OEX_1YML027W S. cerevisiae 11552 Cytoplasmic — 1 129 NUE_OEX_1 YML065W S.cerevisiae 11569 Cytoplasmic — 1 130 NUE_OEX_1 YML089C S. cerevisiae11596 Cytoplasmic — 1 131 NUE_OEX_1 YML128C S. cerevisiae 11600Cytoplasmic — 1 132 NUE_OEX_1 YMR011W S. cerevisiae 11612 Cytoplasmic12124, 12126, 12128, 12130, 12132, 12134, 12136, 12138, 12140, 12142,12144, 12146, 12148, 12150, 12152, 12154, 12156, 12158, 12160, 12162,12164, 12166, 12168, 12170, 12172, 12174, 12176, 12178, 12180, 12182,12184, 12186, 12188, 12190, 12192, 12194, 12196, 12198, 12200, 12202,12204, 12206, 12208, 12210, 12212, 12214, 12216, 12218, 12220, 12222,12224, 12226, 12228, 12230, 12232, 12234, 12236, 12238, 12240 1 133NUE_OEX_1 YMR037C S. cerevisiae 12246 Cytoplasmic — 1 134 NUE_OEX_1YMR049C S. cerevisiae 12263 Cytoplasmic — 1 135 NUE_OEX_1 YMR052W S.cerevisiae 12316 Cytoplasmic — 1 136 NUE_OEX_1 YMR082C S. cerevisiae 12327* Cytoplasmic — 1 137 NUE_OEX_1 YMR125W S. cerevisiae 12331Cytoplasmic — 1 138 NUE_OEX_1 YMR126C S. cerevisiae 12378 Cytoplasmic —1 139 NUE_OEX_1 YMR144W S. cerevisiae 12394 Cytoplasmic — 1 140NUE_OEX_1 YMR160W S. cerevisiae 12406 Cytoplasmic — 1 141 NUE_OEX_1YMR191W S. cerevisiae 12414 Cytoplasmic — 1 142 NUE_OEX_1 YMR209C S.cerevisiae 12420 Cytoplasmic — 1 143 NUE_OEX_1 YMR233W S. cerevisiae12440 Cytoplasmic — 1 144 NUE_OEX_1 YMR278W S. cerevisiae 12470Cytoplasmic — 1 145 NUE_OEX_1 YMR280C S. cerevisiae 12749 Cytoplasmic —1 146 NUE_OEX_1 YNL014W S. cerevisiae 12773 Cytoplasmic — 1 147NUE_OEX_1 YNL320W S. cerevisiae 12829 Cytoplasmic 12867, 12869, 12871,12873 1 148 NUE_OEX_1 YOL007C S. cerevisiae 12883 Cytoplasmic — 1 149NUE_OEX_1 YOL164W S. cerevisiae 12889 Cytoplasmic — 1 150 NUE_OEX_1YOR076C S. cerevisiae 13014 Cytoplasmic — 1 151 NUE_OEX_1 YOR083W S.cerevisiae 13018 Cytoplasmic — 1 152 NUE_OEX_1 YOR097C S. cerevisiae13024 Cytoplasmic — 1 153 NUE_OEX_1 YOR128C S. cerevisiae 13030Cytoplasmic 13098 1 154 NUE_OEX_1 YOR353C S. cerevisiae 14085Cytoplasmic — 1 155 NUE_OEX_1 YPL141C S. cerevisiae 14093 Cytoplasmic —1 156 NUE_OEX_1 YPR088C S. cerevisiae 14113 Cytoplasmic 14215, 14217,14219, 14221, 14223, 14225, 14227, 14229, 14231, 14233 1 157 NUE_OEX_1YPR108W S. cerevisiae 14246 Cytoplasmic 14290, 14292, 14294, 14296,14298 1 158 NUE_OEX_1 YPR110C S. cerevisiae 14311 Cytoplasmic 14373,14375, 14377, 14379, 14381 1 159 NUE_OEX_1 B3825_2 E. coli 14914Plastidic — 1 160 NUE_OEX_1 YIR034C_2 S. cerevisiae 15382 Cytoplasmic —1 161 NUE_OEX_1 YJR131W_2 S. cerevisiae 15460 Cytoplasmic 15556, 15558,15560, 15562 1 162 NUE_OEX_1 YKL100C_2 S. cerevisiae 15571 Cytoplasmic —1 163 NUE_OEX_1 YKL193C_2 S. cerevisiae 15593 Cytoplasmic 15631, 15633,15635, 15637 1 164 NUE_OEX_1 YLL016W_2 S. cerevisiae 15646 Cytoplasmic —1 165 NUE_OEX_1 YLR034C_2 S. cerevisiae 15673 Cytoplasmic 15977, 15979,15981, 15983, 15985, 15987, 15989, 15991, 15993, 15995 1 166 NUE_OEX_1YLR060W_2 S. cerevisiae 16005 Cytoplasmic — 1 167 NUE_OEX_1 YMR082C_2 S.cerevisiae 16114 Cytoplasmic — 1 168 NUE_OEX_1 B1258 E. coli 14402Cytoplasmic — 1 169 NUE_OEX_1 YML101C S. cerevisiae 16093 Cytoplasmic —1 170 NUE_OEX_1 YMR065W S. cerevisiae 16106 Cytoplasmic — 1 171NUE_OEX_1 YMR163C S. cerevisiae 16120 Cytoplasmic — 1 172 NUE_OEX_1YOL042W S. cerevisiae 16275 Cytoplasmic — 1 173 NUE_OEX_1 YOR226C S.cerevisiae 16305 Cytoplasmic 16537, 16539, 16541, 16543, 16545, 16547,16549, 16551, 16553, 16555, 16557, 16559, 16561, 16563, 16565 1 174NUE_OEX_1 YPL068C S. cerevisiae 16573 Cytoplasmic — 1 175 NUE_OEX_1B0165 E. coli 14396 Plastidic — 1 176 NUE_OEX_1 YOR203W S. cerevisiae16299 Cytoplasmic — 1 177 NUE_OEX_1 YNL147W S. cerevisiae 16133Cytoplasmic 16257, 16259, 16261, 16263, 16265, 16267, 16269 1 178NUE_OEX_1 YBR083W S. cerevisiae 15056 Cytoplasmic — 1 179 NUE_OEX_1YKL111C S. cerevisiae 15587 Cytoplasmic — 1 180 NUE_OEX_1 YPR067W S.cerevisiae 16582 Cytoplasmic — 1 181 NUE_OEX_1 B1985 E. coli 14839Cytoplasmic — 1 182 NUE_OEX_1 B3838 E. coli 15014 Cytoplasmic — 1 183NUE_OEX_1 YJL010C S. cerevisiae 15432 Cytoplasmic — 1 184 NUE_OEX_1B1267 E. coli 14497 Cytoplasmic 14709, 14711 1 185 NUE_OEX_1 B1322 E.coli 14718 Cytoplasmic — 1 186 NUE_OEX_1 B1381 E. coli 14791 Cytoplasmic— 1 187 NUE_OEX_1 B2646 E. coli 14879 Cytoplasmic — 1 188 NUE_OEX_1YBR191W S. cerevisiae 15064 Cytoplasmic 15218, 15220, 15222, 15224,15226, 15228, 15230, 15232, 15234, 15236, 15238, 15240, 15242, 15244,15246, 15248 1 189 NUE_OEX_1 YDL135C S. cerevisiae 15257 Cytoplasmic15357, 15359, 15361, 15363, 15365, 15367, 15369, 15371 1 190 NUE_OEX_1YHL005C S. cerevisiae 15378 Cytoplasmic — 1 191 NUE_OEX_1 YKR100C_2 S.cerevisiae 16629 Cytoplasmic — 1 192 NUE_OEX_1 YMR191W_2 S. cerevisiae16647 Cytoplasmic —

TABLE IIA Amino acid sequence ID numbers Ap- 5. plica- 1. 2. 3. 4. Lead6. 7. tion Hit Project Locus Organism SEQ ID Target SEQ IDs ofPolypeptide Homologs 1 1 NUE_OEX_1 B0017 E. coli 39 Cytoplasmic — 1 2NUE_OEX_1 B0045 E. coli 43 Cytoplasmic 45, 47, 49, 51, 53, 55, 57, 59,61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95,97 1 3 NUE_OEX_1 B0180 E. coli 124 Plastidic 126, 128, 130, 132, 134,136, 138, 140, 142, 144, 146, 148, 150, 152, 154, 156, 158, 160, 162,164, 166, 168, 170, 172, 174, 176, 178, 180, 182, 184, 186, 188, 190,192, 194, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218,220, 222, 224, 226, 228, 230, 232, 234, 236, 238, 240, 242, 244, 246,248, 250, 252, 254, 256, 258, 260, 262, 264, 266, 268, 270, 272, 274,276, 278, 280, 282, 284, 286, 288, 290, 292, 294, 296, 298, 300, 302,304, 306, 308, 310, 312, 314, 316, 318, 320, 322, 324, 326, 328, 330,332, 334, 336, 338, 340, 342, 344, 346, 348, 350, 352, 354, 356, 358,360, 362, 364 1 4 NUE_OEX_1 B0242 E. coli 381 Plastidic 383, 385, 387,389, 391, 393, 395, 397, 399, 401, 403, 405, 407, 409, 411, 413, 415,417, 419, 421, 423, 425, 427, 429, 431, 433, 435, 437, 439, 441, 443,445, 447, 449, 451, 453, 455, 457, 459, 461, 463, 465, 467, 469, 471,473, 475, 477, 479, 481, 483, 485, 487, 489, 491, 493, 495, 497, 499,501, 503, 505, 507, 509, 511, 513, 515, 517, 519, 521, 523, 525, 527,529, 531, 533, 535, 537, 539, 541, 543, 545, 547, 549, 551, 553, 555,557, 559, 561, 563, 565, 567, 569, 571, 573, 575, 577, 579, 581, 583,585, 587, 589, 591, 593, 595, 597, 599, 601, 603, 605, 607, 609, 611,613, 615, 617, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639,641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661 1 5 NUE_OEX_1B0403 E. coli 680 Plastidic 682, 684, 686, 688, 690, 692, 694, 696, 698,700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726,728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754,756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782,784, 786, 788, 790, 792, 794, 796, 798, 800 1 6 NUE_OEX_1 B0474 E. coli813 Cytoplasmic 815, 817, 819, 821, 823, 825, 827, 829, 831, 833, 835,837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863,865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891,893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919,921, 923, 925, 927, 929, 931, 933, 935, 937, 939, 941, 943, 945, 947,949, 951, 953, 955, 957 1 7 NUE_OEX_1 B0754 E. coli 1056 Plastidic 1058,1060, 1062, 1064, 1066, 1068, 1070, 1072, 1074, 1076, 1078, 1080, 1082,1084, 1086, 1088, 1090, 1092, 1094, 1096, 1098, 1100, 1102, 1104, 1106,1108, 1110, 1112, 1114, 1116, 1118, 1120, 1122, 1124, 1126, 1128, 1130,1132, 1134, 1136, 1138, 1140, 1142, 1144, 1146, 1148, 1150, 1152, 1154,1156, 1158, 1160, 1162, 1164, 1166, 1168, 1170, 1172, 1174, 1176, 1178,1180, 1182, 1184, 1186, 1188, 1190, 1192, 1194, 1196, 1198, 1200, 1202,1204, 1206, 1208, 1210, 1212, 1214, 1216, 1218, 1220, 1222, 1224, 1226,1228, 1230, 1232, 1234, 1236, 1238, 1240, 1242, 1244, 1246, 1248, 1250,1252, 1254, 1256, 1258, 1260, 1262, 1264, 1266, 1268, 1270, 1272, 1274,1276, 1278, 1280, 1282, 1284, 1286, 1288, 1290, 1292, 1294, 1296, 1298,1300, 1302, 1304, 1306, 1308, 1310, 1312, 1314, 1316, 1318, 1320, 1322,1324, 1326, 1328, 1330, 1332, 1334, 1336, 1338, 1340, 1342, 1344, 1346,1348, 1350, 1352, 1354, 1356, 1358, 1360, 1362, 1364, 1366, 1368, 1370,1372, 1374, 1376, 1378, 1380, 1382, 1384, 1386, 1388, 1390, 1392, 1394,1396, 1398, 1400, 1402, 1404, 1406, 1408, 1410, 1412, 1414, 1416, 1418,1420, 1422, 1424, 1426, 1428, 1430, 1432, 1434, 1436, 1438, 1440, 1442,1444, 1446, 1448, 1450, 1452, 1454, 1456, 1458, 1460, 1462, 1464, 1466,1468, 1470, 1472, 1474, 1476, 1478, 1480, 1482, 1484, 1486, 1488, 1490,1492, 1494, 1496, 1498, 1500, 1502, 1504, 1506, 1508, 1510, 1512, 1514,1516, 1518, 1520, 1522, 1524, 1526, 1528, 1530, 1532, 1534, 1536, 1538,1540, 1542, 1544, 1546, 1548, 1550 1 8 NUE_OEX_1 B0784 E. coli 1564Cytoplasmic 1566, 1568, 1570, 1572, 1574, 1576, 1578, 1580, 1582, 1584,1586, 1588, 1590, 1592, 1594, 1596, 1598, 1600, 1602, 1604, 1606, 1608,1610, 1612, 1614, 1616, 1618, 1620, 1622, 1624, 1626, 1628, 1630, 1632,1634, 1636, 1638, 1640, 1642, 1644, 1646, 1648, 1650, 1652, 1654, 1656,1658, 1660, 1662, 1664, 1666, 1668, 1670, 1672, 1674, 1676, 1678, 1680,1682, 1684, 1686, 1688, 1690, 1692, 1694, 1696, 1698, 1700 1 9 NUE_OEX_1B0873 E. coli 1706 Plastidic 1708, 1710, 1712, 1714, 1716, 1718, 1720,1722, 1724, 1726, 1728, 1730, 1732, 1734, 1736, 1738, 1740, 1742, 1744,1746, 1748, 1750, 1752, 1754, 1756, 1758, 1760, 1762, 1764, 1766, 1768,1770, 1772, 1774, 1776, 1778, 1780, 1782, 1784, 1786, 1788, 1790, 1792,1794, 1796, 1798, 1800, 1802, 1804, 1806, 1808, 1810, 1812, 1814, 1816,1818, 1820, 1822, 1824, 1826, 1828, 1830 1 10 NUE_OEX_1 B1014 E. coli1845 Cytoplasmic 1847, 1849, 1851, 1853, 1855, 1857, 1859, 1861, 1863,1865, 1867, 1869, 1871, 1873, 1875, 1877, 1879, 1881, 1883, 1885, 1887,1889, 1891, 1893, 1895, 1897, 1899, 1901, 1903, 1905, 1907, 1909, 1911,1913, 1915, 1917, 1919, 1921, 1923, 1925, 1927, 1929, 1931 1 11NUE_OEX_1 B1020 E. coli 1951 Plastidic 1953, 1955, 1957, 1959, 1961,1963, 1965 1 12 NUE_OEX_1 B1180 E. coli 1976 Cytoplasmic 1978, 1980,1982, 1984, 1986, 1988, 1990, 1992, 1994, 1996, 1998, 2000, 2002, 2004,2006, 2008, 2010, 2012, 2014, 2016, 2018, 2020, 2022, 2024, 2026, 2028,2030, 2032, 2034, 2036, 2038, 2040, 2042, 2044, 2046, 2048, 2050, 2052,2054, 2056, 2058, 2060, 2062, 2064, 2066, 2068, 2070, 2072, 2074, 2076,2078, 2080, 2082, 2084, 2086, 2088, 2090, 2092, 2094, 2096, 2098 1 13NUE_OEX_1 B1933 E. coli 2128 Plastidic 2130, 2132 1 14 NUE_OEX_1 B2032E. coli 2136 Plastidic 2138, 2140, 2142, 2144, 2146, 2148, 2150, 2152,2154, 2156, 2158, 2160, 2162, 2164, 2166 1 15 NUE_OEX_1 B2165 E. coli2172 Plastidic 2174, 2176, 2178, 2180, 2182, 2184, 2186, 2188, 2190,2192, 2194, 2196, 2198, 2200, 2202, 2204, 2206, 2208, 2210, 2212, 2214,2216, 2218, 2220, 2222, 2224, 2226, 2228, 2230, 2232, 2234, 2236, 2238,2240, 2242, 2244, 2246, 2248, 2250, 2252, 2254, 2256, 2258, 2260, 2262,2264, 2266, 2268, 2270, 2272, 2274, 2276, 2278, 2280, 2282, 2284 1 16NUE_OEX_1 B2223 E. coli 2298 Plastidic 2300, 2302, 2304, 2306, 2308,2310, 2312, 2314, 2316, 2318, 2320, 2322, 2324, 2326, 2328, 2330, 2332,2334, 2336, 2338, 2340, 2342, 2344, 2346, 2348, 2350, 2352, 2354, 2356,2358, 2360, 2362, 2364, 2366, 2368, 2370, 2372, 2374, 2376, 2378, 2380,2382, 2384, 2386, 2388, 2390, 2392, 2394, 2396, 2398, 2400, 2402, 2404,2406, 2408, 2410, 2412, 2414, 2416, 2418 1 17 NUE_OEX_1 B2238 E. coli2427 Plastidic 2429, 2431, 2433, 2435, 2437, 2439, 2441, 2443 1 17NUE_OEX_1 B2238 E. coli 2427 Cytoplasmic 2429, 2431, 2433, 2435, 2437,2439, 2441, 2443 1 18 NUE_OEX_1 B2310 E. coli 2453 Plastidic 2455, 2457,2459, 2461, 2463, 2465, 2467, 2469, 2471, 2473, 2475, 2477, 2479, 2481,2483, 2485, 2487, 2489, 2491, 2493, 2495, 2497, 2499, 2501, 2503, 2505,2507, 2509, 2511, 2513, 2515, 2517, 2519, 2521, 2523, 2525, 2527, 2529,2531, 2533, 2535, 2537, 2539, 2541, 2543 1 19 NUE_OEX_1 B2431 E. coli2552 Plastidic 2554, 2556, 2558, 2560, 2562, 2564, 2566, 2568, 2570,2572, 2574, 2576, 2578, 2580, 2582, 2584, 2586, 2588, 2590 1 20NUE_OEX_1 B2600 E. coli 2601 Plastidic 2603, 2605, 2607, 2609, 2611,2613, 2615, 2617, 2619, 2621, 2623, 2625, 2627, 2629, 2631, 2633, 2635,2637, 2639, 2641, 2643, 2645, 2647, 2649, 2651, 2653, 2655, 2657 1 21NUE_OEX_1 B2766 E. coli 2669 Plastidic 2671, 2673, 2675, 2677, 2679,2681, 2683, 2685, 2687, 2689, 2691, 2693, 2695, 2697, 2699, 2701, 2703,2705, 2707, 2709, 2711, 2713, 2715, 2717, 2719, 2721, 2723, 2725, 2727,2729, 2731, 2733, 2735, 2737, 2739, 2741, 2743, 2745, 2747, 2749, 2751,2753, 2755, 2757, 2759, 2761, 2763, 2765 1 22 NUE_OEX_1 B2903 E. coli2773 Cytoplasmic 2775, 2777, 2779, 2781, 2783, 2785, 2787, 2789, 2791,2793, 2795, 2797, 2799, 2801, 2803, 2805, 2807, 2809, 2811, 2813, 2815,2817, 2819, 2821, 2823, 2825, 2827, 2829, 2831, 2833, 2835, 2837, 2839,2841, 2843, 2845, 2847, 2849, 2851, 2853, 2855, 2857, 2859, 2861, 2863,2865, 2867, 2869, 2871, 2873, 2875, 2877, 2879, 2881, 2883, 2885, 2887,2889, 2891, 2893, 2895, 2897, 2899, 2901, 2903, 2905, 2907, 2909, 2911,2913, 2915, 2917, 2919, 2921, 2923, 2925, 2927, 2929, 2931, 2933, 2935,2937, 2939, 2941, 2943, 2945, 2947, 2949, 2951, 2953, 2955, 2957, 2959,2961, 2963, 2965, 2967, 2969, 2971, 2973, 2975, 2977, 2979, 2981, 2983,2985, 2987, 2989, 2991, 2993, 2995, 2997, 2999, 3001, 3003, 3005, 3007,3009, 3011, 3013, 3015, 3017, 3019, 3021, 3023, 3025, 3027, 3029, 3031,3033, 3035, 3037, 3039, 3041, 3043, 3045, 3047, 3049, 3051, 3053, 3055,3057, 3059, 3061, 3063, 3065, 3067, 3069, 3071, 3073, 3075, 3077, 3079,3081, 3083, 3085, 3087, 3089, 3091, 3093, 3095 1 23 NUE_OEX_1 B3117 E.coli 3118 Plastidic 3120, 3122, 3124, 3126, 3128, 3130, 3132, 3134,3136, 3138, 3140, 3142, 3144, 3146, 3148, 3150, 3152, 3154, 3156, 3158,3160, 3162, 3164, 3166, 3168, 3170, 3172, 3174, 3176, 3178, 3180, 3182,3184, 3186, 3188, 3190, 3192, 3194, 3196, 3198, 3200, 3202, 3204, 3206,3208, 3210, 3212, 3214, 3216, 3218, 3220, 3222, 3224, 3226, 3228, 3230,3232, 3234, 3236, 3238, 3240, 3242, 3244, 3246, 3248, 3250, 3252, 3254,3256, 3258, 3260, 3262, 3264, 3266, 3268, 3270, 3272, 3274, 3276, 3278,3280, 3282, 3284, 3286, 3288, 3290, 3292, 3294, 3296, 3298, 3300, 3302,3304, 3306, 3308, 3310, 3312, 3314, 3316, 3318, 3320, 3322, 3324, 3326,3328, 3330, 3332, 3334, 3336, 3338, 3340, 3342, 3344, 3346, 3348, 3350,3352, 3354, 3356, 3358, 3360, 3362, 3364, 3366, 3368, 3370, 3372 1 24NUE_OEX_1 B3120 E. coli 3391 Plastidic 3393 1 25 NUE_OEX_1 B3216 E. coli3397 Plastidic 3399, 3401, 3403, 3405, 3407, 3409, 3411, 3413, 3415,3417, 3419, 3421, 3423, 3425, 3427, 3429, 3431, 3433, 3435, 3437, 3439,3441, 3443, 3445, 3447, 3449, 3451, 3453, 3455, 3457, 3459, 3461, 3463,3465 1 26 NUE_OEX_1 B3451 E. coli 3471 Plastidic 3473, 3475, 3477, 3479,3481, 3483, 3485, 3487, 3489, 3491, 3493, 3495, 3497, 3499, 3501, 3503,3505, 3507, 3509, 3511, 3513, 3515, 3517, 3519, 3521, 3523, 3525, 3527,3529, 3531, 3533, 3535, 3537, 3539, 3541, 3543, 3545, 3547, 3549, 3551,3553, 3555 1 27 NUE_OEX_1 B3791 E. coli 3564 Cytoplasmic 3566, 3568,3570, 3572, 3574, 3576, 3578, 3580, 3582, 3584, 3586, 3588, 3590, 3592,3594, 3596, 3598, 3600, 3602, 3604, 3606, 3608, 3610, 3612, 3614, 3616,3618, 3620, 3622, 3624, 3626, 3628, 3630, 3632, 3634, 3636, 3638, 3640,3642, 3644, 3646, 3648, 3650, 3652, 3654, 3656, 3658, 3660, 3662, 3664,3666, 3668, 3670, 3672, 3674, 3676, 3678, 3680, 3682, 3684, 3686, 3688,3690, 3692, 3694, 3696, 3698, 3700, 3702, 3704, 3706, 3708, 3710, 3712,3714, 3716, 3718, 3720, 3722, 3724, 3726, 3728, 3730, 3732, 3734, 3736,3738, 3740, 3742, 3744, 3746, 3748, 3750, 3752, 3754, 3756, 3758, 3760,3762, 3764 1 28 NUE_OEX_1 B3825 E. coli 3771 Plastidic 3773, 3775, 3777,3779, 3781, 3783, 3785, 3787, 3789, 3791, 3793, 3795, 3797, 3799, 3801,3803, 3805, 3807, 3809, 3811, 3813, 3815, 3817, 3819, 3821, 3823, 3825,3827, 3829, 3831, 3833, 3835, 3837, 3839, 3841, 3843, 3845, 3847, 3849,3851, 3853, 3855, 3857, 3859, 3861, 3863 1 29 NUE_OEX_1 YAL019W S.cerevisiae 3869 Cytoplasmic 3871, 3873, 3875, 3877 1 30 NUE_OEX_1YAR035W S. cerevisiae 3896 Cytoplasmic 3898, 3900, 3902, 3904, 3906,3908, 3910, 3912, 3914, 3916, 3918, 3920, 3922, 3924, 3926, 3928, 3930,3932, 3934, 3936, 3938, 3940 1 31 NUE_OEX_1 YBL021C S. cerevisiae 3954Cytoplasmic 3956, 3958, 3960, 3962, 3964, 3966, 3968, 3970, 3972, 3974,3976, 3978, 3980, 3982, 3984, 3986, 3988, 3990, 3992, 3994, 3996, 3998,4000, 4002, 4004, 4006, 4008, 4010, 4012, 4014, 4016, 4018, 4020, 4022,4024, 4026, 4028, 4030 1 32 NUE_OEX_1 YBR055C S. cerevisiae 4112Cytoplasmic 4114, 4116, 4118, 4120, 4122, 4124, 4126, 4128, 4130, 4132,4134, 4136, 4138, 4140 1 33 NUE_OEX_1 YBR128C S. cerevisiae 4150Cytoplasmic 4152, 4154, 4156 1 34 NUE_OEX_1 YBR159W S. cerevisiae 4163Cytoplasmic 4165, 4167, 4169, 4171, 4173, 4175, 4177, 4179, 4181, 4183,4185, 4187, 4189, 4191, 4193, 4195, 4197, 4199, 4201, 4203, 4205, 4207,4209, 4211, 4213 1 35 NUE_OEX_1 YBR243C S. cerevisiae 4236 Cytoplasmic4238, 4240, 4242, 4244, 4246, 4248, 4250, 4252, 4254, 4256, 4258, 4260,4262, 4264, 4266 1 35 NUE_OEX_1 YBR243C S. cerevisiae 4236 Plastidic4238, 4240, 4242, 4244, 4246, 4248, 4250, 4252, 4254, 4256, 4258, 4260,4262, 4264, 4266 1 36 NUE_OEX_1 YBR262C S. cerevisiae 4281 Cytoplasmic4283, 4285 1 37 NUE_OEX_1 YCR019W S. cerevisiae 4289 Cytoplasmic 4291,4293, 4295, 4297, 4299, 4301, 4303, 4305 1 38 NUE_OEX_1 YDR070C S.cerevisiae 4316 Cytoplasmic 4318, 4320 1 39 NUE_OEX_1 YDR079W S.cerevisiae 4326 Cytoplasmic 4328, 4330 1 40 NUE_OEX_1 YDR123C S.cerevisiae 4336 Cytoplasmic 4338, 4340 1 41 NUE_OEX_1 YDR137W S.cerevisiae 4347 Cytoplasmic 4349, 4351 1 42 NUE_OEX_1 YDR294C S.cerevisiae 4362 Cytoplasmic 4364, 4366, 4368, 4370, 4372, 4374, 4376,4378, 4380, 4382, 4384, 4386, 4388, 4390 1 42 NUE_OEX_1 YDR294C S.cerevisiae 4362 Plastidic 4364, 4366, 4368, 4370, 4372, 4374, 4376,4378, 4380, 4382, 4384, 4386, 4388, 4390 1 43 NUE_OEX_1 YDR330W S.cerevisiae 4403 Cytoplasmic 4405, 4407, 4409, 4411, 4413, 4415, 4417,4419, 4421, 4423 1 44 NUE_OEX_1 YDR355C S. cerevisiae 4432 Cytoplasmic —1 45 NUE_OEX_1 YDR430C S. cerevisiae 4436 Plastidic 4438, 4440, 4442,4444, 4446, 4448, 4450, 4452, 4454, 4456, 4458, 4460, 4462, 4464, 4466,4468 1 46 NUE_OEX_1 YDR472W S. cerevisiae 4486 Cytoplasmic 4488, 4490,4492, 4494, 4496 1 47 NUE_OEX_1 YDR497C S. cerevisiae 4507 Plastidic4509, 4511, 4513, 4515, 4517, 4519, 4521, 4523, 4525, 4527, 4529, 4531,4533, 4535, 4537, 4539, 4541, 4543, 4545, 4547, 4549, 4551, 4553, 4555,4557, 4559, 4561, 4563, 4565, 4567, 4569, 4571, 4573, 4575, 4577, 4579,4581, 4583, 4585, 4587, 4589, 4591, 4593, 4595, 4597, 4599, 4601, 4603,4605, 4607, 4609, 4611, 4613, 4615, 4617, 4619, 4621, 4623, 4625, 4627,4629, 4631, 4633, 4635, 4637, 4639, 4641, 4643, 4645, 4647, 4649, 4651,4653, 4655, 4657, 4659, 4661, 4663, 4665, 4667, 4669, 4671, 4673, 4675,4677, 4679, 4681, 4683, 4685, 4687, 4689, 4691, 4693, 4695, 4697, 4699,4701, 4703, 4705, 4707, 4709, 4711, 4713, 4715, 4717, 4719, 4721, 4723,4725, 4727, 4729, 4731, 4733, 4735, 4737 1 48 NUE_OEX_1 YER029C S.cerevisiae 4791 Cytoplasmic 4793, 4795, 4797, 4799 1 49 NUE_OEX_1YFR007W S. cerevisiae 4807 Cytoplasmic 4809, 4811, 4813, 4815, 4817,4819, 4821, 4823, 4825, 4827, 4829 1 50 NUE_OEX_1 YGL039W S. cerevisiae4837 Cytoplasmic 4839, 4841, 4843, 4845, 4847, 4849, 4851, 4853, 4855,4857, 4859, 4861, 4863, 4865, 4867, 4869, 4871, 4873, 4875, 4877, 4879,4881, 4883, 4885, 4887, 4889, 4891, 4893, 4895, 4897, 4899, 4901, 4903,4905, 4907, 4909, 4911, 4913, 4915, 4917, 4919, 4921, 4923, 4925, 4927,4929, 4931, 4933, 4935, 4937, 4939, 4941, 4943, 4945, 4947, 4949, 4951,4953, 4955, 4957, 4959, 4961, 4963, 4965, 4967, 4969, 4971, 4973, 4975,4977, 4979, 4981, 4983, 4985, 4987, 4989, 4991, 4993, 4995, 4997, 4999,5001, 5003, 5005, 5007, 5009, 5011, 5013, 5015, 5017, 5019, 5021, 5023,5025, 5027, 5029, 5031, 5033, 5035, 5037, 5039, 5041, 5043, 5045, 5047,5049, 5051, 5053, 5055, 5057, 5059, 5061, 5063, 5065, 5067, 5069, 5071,5073, 5075, 5077, 5079, 5081, 5083, 5085, 5087, 5089, 5091, 5093, 5095,5097, 5099, 5101, 5103, 5105, 5107, 5109, 5111, 5113, 5115, 5117, 5119,5121, 5123, 5125, 5127, 5129, 5131, 5133, 5135, 5137, 5139, 5141, 5143,5145, 5147, 5149, 5151, 5153, 5155, 5157, 5159, 5161, 5163, 5165, 5167,5169, 5171, 5173, 5175, 5177, 5179, 5181, 5183, 5185, 5187, 5189, 5191,5193, 5195, 5197, 5199, 5201, 5203, 5205, 5207, 5209, 5211, 5213 1 51NUE_OEX_1 YGL043W S. cerevisiae 5312 Cytoplasmic 5314, 5316, 5318, 5320,5322, 5324, 5326, 5328, 5330, 5332, 5334 1 52 NUE_OEX_1 YGR088W S.cerevisiae 5347 Cytoplasmic 5349, 5351, 5353, 5355, 5357, 5359, 5361,5363, 5365, 5367, 5369, 5371, 5373, 5375, 5377, 5379, 5381, 5383, 5385,5387, 5389, 5391, 5393, 5395, 5397, 5399, 5401, 5403, 5405, 5407, 5409,5411, 5413, 5415, 5417, 5419, 5421, 5423, 5425, 5427, 5429, 5431, 5433,5435, 5437, 5439, 5441, 5443, 5445, 5447, 5449, 5451, 5453, 5455, 5457,5459, 5461, 5463, 5465, 5467, 5469, 5471, 5473, 5475, 5477, 5479, 5481,5483, 5485, 5487, 5489, 5491, 5493, 5495, 5497, 5499, 5501, 5503, 5505,5507, 5509, 5511, 5513, 5515, 5517, 5519, 5521, 5523 1 53 NUE_OEX_1YGR122C-A S. cerevisiae 5534 Cytoplasmic 5536, 5538, 5540, 5542, 5544,5546 1 54 NUE_OEX_1 YGR142W S. cerevisiae 5552 Cytoplasmic 5554, 5556 155 NUE_OEX_1 YGR143W S. cerevisiae 5560 Cytoplasmic 5562, 5564, 5566,5568, 5570, 5572, 5574, 5576, 5578, 5580, 5582, 5584, 5586 1 56NUE_OEX_1 YGR165W S. cerevisiae 5603 Cytoplasmic 5605 1 57 NUE_OEX_1YGR170W S. cerevisiae 5609 Cytoplasmic 5611 1 58 NUE_OEX_1 YGR202C S.cerevisiae 5615 Cytoplasmic 5617, 5619, 5621, 5623, 5625, 5627, 5629,5631, 5633, 5635, 5637, 5639, 5641, 5643, 5645, 5647, 5649, 5651, 5653,5655, 5657, 5659 1 59 NUE_OEX_1 YGR266W S. cerevisiae 5667 Cytoplasmic5669, 5671, 5673, 5675, 5677, 5679, 5681, 5683, 5685, 5687 1 60NUE_OEX_1 YGR282C S. cerevisiae 5702 Cytoplasmic 5704, 5706, 5708, 5710,5712, 5714, 5716, 5718, 5720, 5722, 5724, 5726, 5728, 5730, 5732, 5734,5736, 5738, 5740 1 61 NUE_OEX_1 YGR290W S. cerevisiae 5751 Cytoplasmic —1 62 NUE_OEX_1 YHL021C S. cerevisiae 5755 Cytoplasmic 5757, 5759, 5761,5763, 5765, 5767, 5769 1 63 NUE_OEX_1 YHL031C S. cerevisiae 5779Cytoplasmic 5781, 5783, 5785, 5787, 5789, 5791, 5793, 5795, 5797, 5799,5801, 5803, 5805, 5807 1 64 NUE_OEX_1 YHR011W S. cerevisiae 5813Cytoplasmic 5815, 5817, 5819, 5821, 5823, 5825, 5827, 5829, 5831, 5833,5835, 5837, 5839, 5841, 5843, 5845, 5847, 5849, 5851, 5853, 5855, 5857,5859, 5861, 5863, 5865, 5867, 5869, 5871, 5873, 5875, 5877, 5879, 5881,5883, 5885, 5887, 5889, 5891, 5893, 5895, 5897, 5899, 5901, 5903, 5905,5907, 5909, 5911, 5913, 5915, 5917, 5919, 5921, 5923, 5925, 5927, 5929,5931, 5933, 5935, 5937, 5939, 5941, 5943, 5945, 5947, 5949, 5951, 5953 165 NUE_OEX_1 YHR127W S. cerevisiae 5968 Cytoplasmic 5970 1 66 NUE_OEX_1YHR137W S. cerevisiae 5974 Cytoplasmic 5976, 5978, 5980, 5982, 5984,5986, 5988, 5990, 5992, 5994, 5996, 5998, 6000, 6002, 6004, 6006, 6008,6010, 6012, 6014, 6016, 6018, 6020 1 66 NUE_OEX_1 YHR137W S. cerevisiae5974 Plastidic 5976, 5978, 5980, 5982, 5984, 5986, 5988, 5990, 5992,5994, 5996, 5998, 6000, 6002, 6004, 6006, 6008, 6010, 6012, 6014, 6016,6018, 6020 1 67 NUE_OEX_1 YIL099W S. cerevisiae 6028 Cytoplasmic 6030,6032, 6034, 6036, 6038, 6040, 6042, 6044, 6046, 6048, 6050, 6052, 6054,6056, 6058, 6060, 6062, 6064, 6066, 6068, 6070, 6072, 6074, 6076, 6078,6080, 6082, 6084, 6086, 6088, 6090, 6092, 6094, 6096, 6098 1 67NUE_OEX_1 YIL099W S. cerevisiae 6028 Plastidic 6030, 6032, 6034, 6036,6038, 6040, 6042, 6044, 6046, 6048, 6050, 6052, 6054, 6056, 6058, 6060,6062, 6064, 6066, 6068, 6070, 6072, 6074, 6076, 6078, 6080, 6082, 6084,6086, 6088, 6090, 6092, 6094, 6096, 6098 1 68 NUE_OEX_1 YIL147C S.cerevisiae 6108 Cytoplasmic 6110, 6112, 6114, 6116, 6118, 6120, 6122,6124, 6126, 6128, 6130, 6132 1 69 NUE_OEX_1 YIR034C S. cerevisiae 6151Cytoplasmic 6153, 6155, 6157, 6159, 6161, 6163, 6165, 6167, 6169, 6171,6173, 6175, 6177, 6179, 6181, 6183, 6185 1 70 NUE_OEX_1 YJL013C S.cerevisiae 6199 Cytoplasmic 6201, 6203, 6205 1 71 NUE_OEX_1 YJL041W S.cerevisiae 6209 Cytoplasmic 6211, 6213, 6215, 6217, 6219, 6221, 6223,6225, 6227, 6229, 6231, 6233, 6235 1 72 NUE_OEX_1 YJL064W S. cerevisiae6243 Cytoplasmic — 1 73 NUE_OEX_1 YJL067W S. cerevisiae 6247 Cytoplasmic— 1 74 NUE_OEX_1 YJL094C S. cerevisiae 6251 Cytoplasmic 6253, 6255,6257, 6259, 6261, 6263, 6265, 6267, 6269, 6271, 6273, 6275, 6277, 6279,6281, 6283, 6285 1 75 NUE_OEX_1 YJL171C S. cerevisiae 6298 Cytoplasmic6300, 6302, 6304, 6306, 6308, 6310, 6312, 6314, 6316 1 76 NUE_OEX_1YJL213W S. cerevisiae 6327 Cytoplasmic 6329, 6331, 6333, 6335, 6337,6339, 6341, 6343, 6345, 6347, 6349, 6351, 6353, 6355, 6357, 6359, 6361,6363, 6365, 6367, 6369, 6371, 6373, 6375, 6377, 6379, 6381, 6383, 6385,6387, 6389, 6391, 6393, 6395, 6397, 6399, 6401, 6403, 6405, 6407, 6409,6411, 6413, 6415, 6417, 6419, 6421, 6423, 6425, 6427, 6429, 6431, 6433,6435, 6437, 6439, 6441, 6443, 6445, 6447, 6449, 6451, 6453, 6455, 6457,6459, 6461, 6463, 6465, 6467, 6469, 6471, 6473, 6475, 6477, 6479, 6481 177 NUE_OEX_1 YJR017C S. cerevisiae 6489 Cytoplasmic 6491, 6493, 6495,6497, 6499, 6501, 6503, 6505, 6507, 6509, 6511, 6513, 6515, 6517, 6519,6521, 6523, 6525, 6527, 6529, 6531, 6533, 6535, 6537, 6539, 6541 1 78NUE_OEX_1 YJR058C S. cerevisiae 6551 Cytoplasmic 6553, 6555, 6557, 6559,6561, 6563, 6565, 6567, 6569, 6571, 6573, 6575, 6577, 6579, 6581, 6583,6585, 6587, 6589, 6591, 6593, 6595, 6597, 6599, 6601, 6603, 6605, 6607,6609, 6611, 6613, 6615, 6617, 6619, 6621, 6623, 6625, 6627, 6629, 6631,6633, 6635, 6637, 6639, 6641, 6643, 6645, 6647, 6649, 6651, 6653, 6655,6657, 6659, 6661 1 79 NUE_OEX_1 YJR117W S. cerevisiae 6701 Cytoplasmic6703, 6705, 6707, 6709, 6711, 6713, 6715, 6717, 6719, 6721, 6723, 6725,6727, 6729, 6731, 6733, 6735, 6737, 6739, 6741, 6743, 6745, 6747, 6749,6751, 6753, 6755, 6757, 6759, 6761, 6763, 6765, 6767, 6769, 6771, 6773,6775, 6777, 6779, 6781, 6783, 6785, 6787, 6789 1 80 NUE_OEX_1 YJR121W S.cerevisiae 6817 Cytoplasmic 6819, 6821, 6823, 6825, 6827, 6829, 6831,6833, 6835, 6837, 6839, 6841, 6843, 6845, 6847, 6849, 6851, 6853, 6855,6857, 6859, 6861, 6863, 6865, 6867, 6869, 6871, 6873, 6875, 6877, 6879,6881, 6883, 6885, 6887, 6889, 6891, 6893, 6895, 6897, 6899, 6901, 6903,6905, 6907, 6909, 6911, 6913, 6915, 6917, 6919, 6921, 6923, 6925, 6927,6929, 6931, 6933, 6935, 6937, 6939, 6941, 6943, 6945, 6947, 6949, 6951,6953, 6955, 6957, 6959, 6961, 6963, 6965, 6967, 6969, 6971, 6973, 6975,6977, 6979, 6981, 6983, 6985, 6987, 6989, 6991, 6993, 6995, 6997, 6999,7001, 7003, 7005, 7007, 7009, 7011, 7013, 7015, 7017, 7019, 7021, 7023,7025, 7027, 7029, 7031, 7033, 7035, 7037, 7039, 7041, 7043, 7045, 7047,7049, 7051, 7053, 7055, 7057, 7059, 7061, 7063, 7065, 7067, 7069, 7071,7073, 7075, 7077, 7079, 7081, 7083, 7085, 7087, 7089, 7091, 7093, 7095,7097, 7099, 7101, 7103, 7105, 7107, 7109, 7111, 7113, 7115, 7117, 7119,7121, 7123, 7125, 7127, 7129, 7131, 7133, 7135, 7137, 7139, 7141, 7143,7145, 7147, 7149, 7151, 7153, 7155, 7157, 7159, 7161, 7163, 7165, 7167,7169, 7171, 7173, 7175, 7177, 7179, 7181, 7183, 7185, 7187, 7189, 7191,7193, 7195, 7197, 7199, 7201, 7203, 7205, 7207, 7209, 7211, 7213, 7215,7217, 7219, 7221, 7223, 7225, 7227, 7229, 7231, 7233, 7235, 7237, 7239,7241, 7243, 7245, 7247, 7249, 7251, 7253, 7255, 7257, 7259, 7261, 7263,7265, 7267, 7269, 7271, 7273, 7275, 7277, 7279, 7281, 7283, 7285, 7287,7289, 7291, 7293, 7295, 7297, 7299, 7301, 7303, 7305, 7307, 7309, 7311,7313, 7315, 7317, 7319, 7321, 7323, 7325, 7327, 7329, 7331, 7333, 7335 181 NUE_OEX_1 YJR131W S. cerevisiae 7367 Cytoplasmic 7369, 7371, 7373,7375, 7377, 7379, 7381, 7383, 7385, 7387, 7389, 7391, 7393, 7395, 7397,7399, 7401, 7403, 7405, 7407, 7409, 7411, 7413, 7415, 7417, 7419, 7421,7423, 7425, 7427, 7429, 7431, 7433, 7435, 7437, 7439, 7441, 7443, 7445,7447, 7449, 7451, 7453, 7455, 7457, 7459 1 82 NUE_OEX_1 YJR145C S.cerevisiae 7476 Cytoplasmic 7478, 7480, 7482, 7484, 7486, 7488, 7490,7492, 7494, 7496, 7498, 7500, 7502, 7504, 7506, 7508, 7510, 7512, 7514,7516, 7518, 7520, 7522, 7524, 7526, 7528, 7530, 7532, 7534, 7536, 7538,7540, 7542, 7544, 7546, 7548, 7550, 7552, 7554, 7556, 7558 1 83NUE_OEX_1 YKL084W S. cerevisiae 7603 Cytoplasmic 7605, 7607, 7609, 7611,7613, 7615, 7617, 7619, 7621, 7623, 7625, 7627, 7629, 7631, 7633, 7635,7637, 7639, 7641, 7643, 7645 1 84 NUE_OEX_1 YKL088W S. cerevisiae 7652Cytoplasmic 7654 1 85 NUE_OEX_1 YKL100C S. cerevisiae 7662 Cytoplasmic7664, 7666, 7668 1 86 NUE_OEX_1 YKL131W S. cerevisiae 7676 Cytoplasmic —1 87 NUE_OEX_1 YKL138C S. cerevisiae 7680 Cytoplasmic 7682, 7684, 7686,7688, 7690, 7692, 7694, 7696, 7698, 7700, 7702, 7704 1 88 NUE_OEX_1YKL178C S. cerevisiae 7711 Cytoplasmic 7713, 7715, 7717, 7719 1 89NUE_OEX_1 YKL179C S. cerevisiae 7736 Cytoplasmic 7738, 7740, 7742, 7744,7746, 7748, 7750, 7752, 7754, 7756, 7758, 7760, 7762, 7764, 7766, 7768 190 NUE_OEX_1 YKL193C S. cerevisiae 7779 Cytoplasmic 7781, 7783, 7785,7787, 7789, 7791, 7793, 7795, 7797, 7799, 7801, 7803, 7805, 7807, 7809,7811, 7813 1 91 NUE_OEX_1 YKL216W S. cerevisiae 7830 Cytoplasmic 7832,7834, 7836, 7838, 7840, 7842, 7844, 7846, 7848, 7850, 7852, 7854, 7856,7858, 7860, 7862, 7864, 7866, 7868, 7870, 7872, 7874, 7876, 7878, 7880,7882, 7884, 7886, 7888, 7890, 7892, 7894, 7896, 7898, 7900, 7902, 7904,7906, 7908, 7910, 7912, 7914, 7916, 7918, 7920, 7922, 7924, 7926, 7928,7930, 7932, 7934, 7936, 7938, 7940, 7942, 7944, 7946, 7948, 7950, 7952,7954, 7956, 7958, 7960, 7962, 7964, 7966, 7968, 7970, 7972, 7974, 7976,7978, 7980, 7982, 7984, 7986, 7988, 7990, 7992, 7994, 7996, 7998, 8000,8002, 8004, 8006, 8008, 8010, 8012 1 92 NUE_OEX_1 YKR016W S. cerevisiae8018 Cytoplasmic 8020, 8022, 8024, 8026, 8028, 8030, 8032, 8034, 8036,8038 1 93 NUE_OEX_1 YKR021W S. cerevisiae 8046 Cytoplasmic 8048, 8050,8052, 8054, 8056, 8058, 8060 1 94 NUE_OEX_1 YKR055W S. cerevisiae 8074Cytoplasmic 8076, 8078, 8080, 8082, 8084, 8086, 8088, 8090, 8092, 8094,8096, 8098, 8100, 8102, 8104, 8106, 8108, 8110, 8112, 8114, 8116, 8118,8120, 8122, 8124, 8126, 8128, 8130, 8132, 8134, 8136, 8138, 8140, 8142,8144, 8146, 8148, 8150, 8152, 8154, 8156, 8158, 8160, 8162, 8164, 8166,8168, 8170, 8172, 8174, 8176, 8178, 8180, 8182, 8184, 8186, 8188, 8190,8192, 8194, 8196, 8198, 8200, 8202, 8204, 8206, 8208, 8210, 8212, 8214,8216, 8218, 8220, 8222, 8224, 8226, 8228, 8230, 8232, 8234, 8236, 8238,8240, 8242, 8244, 8246, 8248, 8250, 8252, 8254, 8256 1 95 NUE_OEX_1YKR088C S. cerevisiae 8264 Plastidic 8266, 8268, 8270, 8272, 8274, 8276,8278, 8280 1 96 NUE_OEX_1 YKR093W S. cerevisiae 8288 Cytoplasmic 8290,8292, 8294, 8296, 8298, 8300, 8302, 8304, 8306, 8308, 8310, 8312, 8314,8316, 8318, 8320, 8322, 8324, 8326, 8328, 8330, 8332, 8334, 8336, 8338,8340, 8342, 8344, 8346, 8348, 8350, 8352, 8354, 8356, 8358, 8360, 8362,8364, 8366, 8368, 8370, 8372, 8374, 8376, 8378, 8380, 8382, 8384, 8386,8388, 8390, 8392, 8394, 8396, 8398, 8400, 8402, 8404, 8406, 8408, 8410,8412, 8414, 8416, 8418, 8420, 8422, 8424, 8426, 8428, 8430, 8432, 8434,8436, 8438, 8440, 8442 1 97 NUE_OEX_1 YKR099W S. cerevisiae 8469Cytoplasmic 8471, 8473 1 98 NUE_OEX_1 YKR100C S. cerevisiae 8485Cytoplasmic 8487, 8489 1 99 NUE_OEX_1 YLL014W S. cerevisiae 8493Cytoplasmic 8495, 8497, 8499, 8501, 8503, 8505, 8507, 8509 1 100NUE_OEX_1 YLL016W S. cerevisiae 8515 Cytoplasmic 8517, 8519, 8521, 8523,8525, 8527 1 101 NUE_OEX_1 YLL023C S. cerevisiae 8540 Cytoplasmic 8542,8544, 8546, 8548, 8550, 8552, 8554, 8556, 8558, 8560, 8562, 8564, 8566 1102 NUE_OEX_1 YLL037W S. cerevisiae 8572 Cytoplasmic — 1 103 NUE_OEX_1YLL049W S. cerevisiae 8576 Cytoplasmic — 1 104 NUE_OEX_1 YLL055W S.cerevisiae 8580 Cytoplasmic 8582, 8584, 8586, 8588, 8590, 8592, 8594,8596, 8598, 8600, 8602, 8604, 8606, 8608, 8610, 8612, 8614, 8616, 8618,8620, 8622, 8624, 8626, 8628, 8630, 8632, 8634, 8636, 8638, 8640, 8642,8644, 8646, 8648, 8650, 8652, 8654, 8656 1 105 NUE_OEX_1 YLR034C S.cerevisiae 8662 Cytoplasmic 8664, 8666, 8668, 8670, 8672, 8674, 8676,8678, 8680, 8682, 8684, 8686, 8688, 8690, 8692, 8694, 8696, 8698, 8700,8702, 8704, 8706, 8708, 8710, 8712, 8714, 8716, 8718, 8720, 8722, 8724,8726, 8728, 8730, 8732, 8734, 8736, 8738, 8740, 8742, 8744, 8746, 8748,8750, 8752, 8754, 8756, 8758, 8760, 8762, 8764, 8766, 8768, 8770, 8772,8774, 8776, 8778, 8780, 8782, 8784, 8786, 8788, 8790, 8792, 8794, 8796,8798, 8800, 8802, 8804, 8806, 8808, 8810, 8812, 8814, 8816, 8818, 8820,8822, 8824, 8826, 8828, 8830, 8832, 8834, 8836, 8838, 8840, 8842, 8844,8846, 8848, 8850, 8852, 8854, 8856, 8858, 8860, 8862, 8864, 8866, 8868,8870, 8872, 8874, 8876, 8878, 8880, 8882, 8884, 8886, 8888, 8890, 8892,8894, 8896, 8898, 8900, 8902, 8904, 8906, 8908, 8910, 8912, 8914, 8916,8918, 8920, 8922, 8924, 8926, 8928, 8930, 8932, 8934, 8936, 8938, 8940,8942, 8944, 8946, 8948, 8950, 8952, 8954, 8956, 8958, 8960, 8962 1 106NUE_OEX_1 YLR042C S. cerevisiae 8992 Cytoplasmic — 1 107 NUE_OEX_1YLR053C S. cerevisiae 8996 Cytoplasmic — 1 108 NUE_OEX_1 YLR058C S.cerevisiae 9000 Cytoplasmic 9002, 9004, 9006, 9008, 9010, 9012, 9014,9016, 9018, 9020, 9022, 9024, 9026, 9028, 9030, 9032, 9034, 9036, 9038,9040, 9042, 9044, 9046, 9048, 9050, 9052, 9054, 9056, 9058, 9060, 9062,9064, 9066, 9068, 9070, 9072, 9074, 9076, 9078, 9080, 9082, 9084, 9086,9088, 9090, 9092, 9094, 9096, 9098, 9100, 9102, 9104, 9106, 9108, 9110,9112, 9114, 9116, 9118, 9120, 9122, 9124, 9126, 9128, 9130, 9132, 9134,9136, 9138, 9140, 9142, 9144, 9146, 9148, 9150, 9152, 9154, 9156, 9158,9160, 9162, 9164, 9166, 9168, 9170, 9172, 9174, 9176, 9178, 9180, 9182,9184, 9186, 9188, 9190, 9192, 9194, 9196, 9198, 9200, 9202, 9204, 9206,9208, 9210, 9212, 9214, 9216, 9218, 9220, 9222, 9224, 9226, 9228, 9230,9232, 9234, 9236, 9238, 9240, 9242, 9244, 9246, 9248, 9250, 9252, 9254,9256, 9258, 9260, 9262, 9264, 9266, 9268, 9270, 9272, 9274, 9276, 9278,9280, 9282, 9284, 9286, 9288, 9290, 9292, 9294, 9296, 9298, 9300, 9302,9304, 9306, 9308, 9310, 9312, 9314, 9316, 9318, 9320, 9322, 9324, 9326,9328, 9330, 9332, 9334, 9336, 9338, 9340, 9342, 9344, 9346, 9348, 9350,9352, 9354, 9356, 9358, 9360, 9362, 9364, 9366, 9368, 9370, 9372, 9374,9376, 9378, 9380, 9382, 9384, 9386, 9388, 9390, 9392, 9394, 9396, 9398,9400, 9402, 9404, 9406, 9408, 9410, 9412, 9414, 9416, 9418, 9420, 9422,9424, 9426, 9428, 9430, 9432, 9434, 9436, 9438, 9440, 9442, 9444, 9446,9448, 9450, 9452, 9454, 9456, 9458, 9460, 9462, 9464, 9466, 9468, 9470,9472, 9474, 9476, 9478, 9480, 9482, 9484, 9486, 9488, 9490, 9492, 9494,9496, 9498, 9500 1 109 NUE_OEX_1 YLR060W S. cerevisiae 9552 Cytoplasmic9554, 9556, 9558, 9560, 9562, 9564, 9566, 9568, 9570, 9572, 9574, 9576,9578, 9580, 9582, 9584, 9586, 9588, 9590, 9592, 9594, 9596, 9598, 9600,9602, 9604, 9606, 9608, 9610, 9612, 9614, 9616, 9618, 9620, 9622, 9624,9626, 9628 1 110 NUE_OEX_1 YLR065C S. cerevisiae 9638 Cytoplasmic 9640,9642, 9644, 9646, 9648, 9650, 9652, 9654, 9656, 9658, 9660, 9662, 9664,9666, 9668 1 111 NUE_OEX_1 YLR070C S. cerevisiae 9673 Cytoplasmic 9675,9677, 9679, 9681, 9683, 9685, 9687, 9689, 9691, 9693, 9695, 9697, 9699,9701, 9703, 9705, 9707, 9709, 9711, 9713, 9715, 9717, 9719, 9721, 9723,9725, 9727, 9729, 9731, 9733, 9735, 9737, 9739, 9741, 9743, 9745, 9747,9749, 9751, 9753, 9755, 9757, 9759, 9761, 9763, 9765, 9767, 9769, 9771,9773, 9775, 9777, 9779, 9781, 9783, 9785, 9787, 9789, 9791, 9793, 9795,9797, 9799, 9801, 9803, 9805, 9807, 9809, 9811, 9813, 9815, 9817, 9819,9821, 9823, 9825, 9827, 9829, 9831, 9833, 9835, 9837, 9839, 9841, 9843,9845, 9847, 9849, 9851, 9853, 9855, 9857, 9859, 9861, 9863, 9865, 9867,9869, 9871, 9873, 9875, 9877, 9879, 9881, 9883, 9885, 9887, 9889, 9891,9893, 9895, 9897, 9899, 9901, 9903, 9905, 9907, 9909, 9911, 9913, 9915,9917, 9919, 9921, 9923, 9925, 9927, 9929, 9931, 9933, 9935, 9937, 9939,9941, 9943, 9945, 9947, 9949, 9951, 9953, 9955, 9957, 9959, 9961, 9963,9965, 9967, 9969, 9971, 9973, 9975, 9977, 9979, 9981, 9983, 9985, 9987,9989, 9991, 9993, 9995, 9997, 9999, 10001, 10003, 10005, 10007, 10009,10011, 10013, 10015, 10017, 10019, 10021, 10023, 10025, 10027, 10029,10031, 10033, 10035, 10037, 10039, 10041, 10043, 10045, 10047, 10049,10051, 10053, 10055, 10057, 10059, 10061, 10063, 10065, 10067, 10069,10071, 10073, 10075, 10077, 10079, 10081, 10083, 10085, 10087, 10089,10091, 10093, 10095, 10097, 10099, 10101, 10103, 10105, 10107, 10109,10111, 10113, 10115, 10117 1 112 NUE_OEX_1 YLR100W S. cerevisiae 10183Cytoplasmic 10185, 10187, 10189, 10191, 10193, 10195, 10197, 10199,10201, 10203 1 113 NUE_OEX_1 YLR109W S. cerevisiae 10215 Cytoplasmic10217, 10219, 10221, 10223, 10225, 10227, 10229, 10231, 10233, 10235,10237, 10239, 10241, 10243, 10245, 10247, 10249, 10251, 10253, 10255,10257, 10259, 10261, 10263, 10265, 10267, 10269, 10271, 10273, 10275,10277, 10279, 10281, 10283, 10285, 10287, 10289, 10291, 10293, 10295,10297, 10299, 10301, 10303, 10305, 10307, 10309, 10311, 10313, 10315,10317, 10319, 10321, 10323, 10325, 10327, 10329, 10331, 10333, 10335,10337, 10339, 10341, 10343, 10345, 10347, 10349, 10351, 10353, 10355,10357, 10359, 10361, 10363, 10365, 10367, 10369, 10371, 10373, 10375,10377, 10379, 10381, 10383, 10385, 10387, 10389, 10391, 10393, 10395,10397, 10399, 10401, 10403, 10405, 10407, 10409, 10411, 10413, 10415,10417 1 114 NUE_OEX_1 YLR125W S. cerevisiae 10448 Cytoplasmic — 1 115NUE_OEX_1 YLR127C S. cerevisiae 10452 Cytoplasmic 10454, 10456, 10458,10460 1 116 NUE_OEX_1 YLR185W S. cerevisiae 10464 Cytoplasmic 10466,10468, 10470, 10472, 10474, 10476, 10478, 10480, 10482, 10484, 10486,10488, 10490, 10492, 10494, 10496, 10498, 10500, 10502, 10504, 10506,10508, 10510, 10512 1 117 NUE_OEX_1 YLR204W S. cerevisiae 10534Cytoplasmic 10536, 10538 1 117 NUE_OEX_1 YLR204W S. cerevisiae 10534Plastidic 10536, 10538 1 118 NUE_OEX_1 YLR242C S. cerevisiae 10542Cytoplasmic 10544, 10546, 10548, 10550, 10552, 10554 1 119 NUE_OEX_1YLR293C S. cerevisiae 10563 Cytoplasmic 10565, 10567, 10569, 10571,10573, 10575, 10577, 10579, 10581, 10583, 10585, 10587, 10589, 10591,10593, 10595, 10597, 10599, 10601, 10603, 10605, 10607, 10609, 10611,10613, 10615, 10617, 10619, 10621, 10623, 10625, 10627, 10629, 10631,10633, 10635, 10637, 10639, 10641, 10643, 10645, 10647, 10649, 10651,10653, 10655, 10657, 10659, 10661, 10663, 10665, 10667, 10669, 10671,10673, 10675, 10677, 10679, 10681, 10683, 10685, 10687, 10689, 10691,10693, 10695, 10697, 10699, 10701, 10703, 10705, 10707, 10709, 10711,10713 1 120 NUE_OEX_1 YLR313C S. cerevisiae 10991 Cytoplasmic 10993,10995 1 121 NUE_OEX_1 YLR315W S. cerevisiae 10999 Cytoplasmic 11001 1122 NUE_OEX_1 YLR329W S. cerevisiae 11005 Cytoplasmic 11007, 11009 1 123NUE_OEX_1 YLR362W S. cerevisiae 11013 Cytoplasmic 11015, 11017, 11019,11021, 11023, 11025, 11027, 11029, 11031, 11033, 11035, 11037, 11039,11041, 11043 1 124 NUE_OEX_1 YLR395C S. cerevisiae 11055 Cytoplasmic11057, 11059, 11061 1 125 NUE_OEX_1 YLR404W S. cerevisiae 11067Cytoplasmic 11069, 11071 1 126 NUE_OEX_1 YLR463C S. cerevisiae 11075Cytoplasmic 11077 1 127 NUE_OEX_1 YML022W S. cerevisiae 11081Cytoplasmic 11083, 11085, 11087, 11089, 11091, 11093, 11095, 11097,11099, 11101, 11103, 11105, 11107, 11109, 11111, 11113, 11115, 11117,11119, 11121, 11123, 11125, 11127, 11129, 11131, 11133, 11135, 11137,11139, 11141, 11143, 11145, 11147, 11149, 11151, 11153, 11155, 11157,11159, 11161, 11163, 11165, 11167, 11169, 11171, 11173, 11175, 11177,11179, 11181, 11183, 11185, 11187, 11189, 11191, 11193, 11195, 11197,11199, 11201, 11203, 11205, 11207, 11209, 11211, 11213, 11215, 11217,11219, 11221, 11223, 11225, 11227, 11229, 11231, 11233, 11235, 11237,11239, 11241, 11243, 11245, 11247, 11249, 11251, 11253, 11255, 11257,11259, 11261, 11263, 11265, 11267, 11269, 11271, 11273, 11275, 11277,11279, 11281, 11283, 11285, 11287, 11289, 11291, 11293, 11295, 11297,11299, 11301, 11303, 11305, 11307, 11309, 11311, 11313, 11315, 11317,11319, 11321, 11323, 11325, 11327, 11329, 11331, 11333, 11335, 11337,11339, 11341, 11343, 11345, 11347, 11349, 11351, 11353, 11355, 11357,11359, 11361, 11363, 11365, 11367, 11369, 11371, 11373, 11375, 11377,11379, 11381, 11383, 11385, 11387, 11389, 11391, 11393, 11395, 11397,11399, 11401, 11403, 11405, 11407, 11409, 11411, 11413, 11415, 11417,11419, 11421, 11423, 11425, 11427, 11429, 11431, 11433, 11435, 11437,11439, 11441, 11443, 11445, 11447, 11449, 11451, 11453, 11455, 11457,11459, 11461, 11463, 11465, 11467, 11469, 11471, 11473, 11475, 11477,11479, 11481, 11483, 11485, 11487, 11489, 11491, 11493, 11495, 11497,11499, 11501, 11503, 11505, 11507, 11509, 11511, 11513, 11515, 11517,11519, 11521, 11523, 11525 1 128 NUE_OEX_1 YML027W S. cerevisiae 11553Cytoplasmic 11555, 11557, 11559, 11561, 11563 1 129 NUE_OEX_1 YML065W S.cerevisiae 11570 Cytoplasmic 11572, 11574, 11576, 11578, 11580, 11582,11584, 11586 1 130 NUE_OEX_1 YML089C S. cerevisiae 11597 Cytoplasmic — 1131 NUE_OEX_1 YML128C S. cerevisiae 11601 Cytoplasmic 11603, 11605,11607, 11609 1 132 NUE_OEX_1 YMR011W S. cerevisiae 11613 Cytoplasmic11615, 11617, 11619, 11621, 11623, 11625, 11627, 11629, 11631, 11633,11635, 11637, 11639, 11641, 11643, 11645, 11647, 11649, 11651, 11653,11655, 11657, 11659, 11661, 11663, 11665, 11667, 11669, 11671, 11673,11675, 11677, 11679, 11681, 11683, 11685, 11687, 11689, 11691, 11693,11695, 11697, 11699, 11701, 11703, 11705, 11707, 11709, 11711, 11713,11715, 11717, 11719, 11721, 11723, 11725, 11727, 11729, 11731, 11733,11735, 11737, 11739, 11741, 11743, 11745, 11747, 11749, 11751, 11753,11755, 11757, 11759, 11761, 11763, 11765, 11767, 11769, 11771, 11773,11775, 11777, 11779, 11781, 11783, 11785, 11787, 11789, 11791, 11793,11795, 11797, 11799, 11801, 11803, 11805, 11807, 11809, 11811, 11813,11815, 11817, 11819, 11821, 11823, 11825, 11827, 11829, 11831, 11833,11835, 11837, 11839, 11841, 11843, 11845, 11847, 11849, 11851, 11853,11855, 11857, 11859, 11861, 11863, 11865, 11867, 11869, 11871, 11873,11875, 11877, 11879, 11881, 11883, 11885, 11887, 11889, 11891, 11893,11895, 11897, 11899, 11901, 11903, 11905, 11907, 11909, 11911, 11913,11915, 11917, 11919, 11921, 11923, 11925, 11927, 11929, 11931, 11933,11935, 11937, 11939, 11941, 11943, 11945, 11947, 11949, 11951, 11953,11955, 11957, 11959, 11961, 11963, 11965, 11967, 11969, 11971, 11973,11975, 11977, 11979, 11981, 11983, 11985, 11987, 11989, 11991, 11993,11995, 11997, 11999, 12001, 12003, 12005, 12007, 12009, 12011, 12013,12015, 12017, 12019, 12021, 12023, 12025, 12027, 12029, 12031, 12033,12035, 12037, 12039, 12041, 12043, 12045, 12047, 12049, 12051, 12053,12055, 12057, 12059, 12061, 12063, 12065, 12067, 12069, 12071, 12073,12075, 12077, 12079, 12081, 12083, 12085, 12087, 12089, 12091, 12093,12095, 12097, 12099, 12101, 12103, 12105, 12107, 12109, 12111, 12113,12115, 12117, 12119, 12121, 12123 1 133 NUE_OEX_1 YMR037C S. cerevisiae12247 Cytoplasmic 12249, 12251, 12253, 12255 1 134 NUE_OEX_1 YMR049C S.cerevisiae 12264 Cytoplasmic 12266, 12268, 12270, 12272, 12274, 12276,12278, 12280, 12282, 12284, 12286, 12288, 12290, 12292, 12294, 12296,12298 1 135 NUE_OEX_1 YMR052W S. cerevisiae 12317 Cytoplasmic 12319,12321 1 136 NUE_OEX_1 YMR082C S. cerevisiae 12328 Cytoplasmic — 1 137NUE_OEX_1 YMR125W S. cerevisiae 12332 Cytoplasmic 12334, 12336, 12338,12340, 12342, 12344, 12346, 12348, 12350, 12352, 12354, 12356, 12358,12360, 12362, 12364, 12366 1 138 NUE_OEX_1 YMR126C S. cerevisiae 12379Cytoplasmic 12381, 12383, 12385 1 139 NUE_OEX_1 YMR144W S. cerevisiae12395 Cytoplasmic 12397, 12399 1 140 NUE_OEX_1 YMR160W S. cerevisiae12407 Cytoplasmic 12409, 12411 1 141 NUE_OEX_1 YMR191W S. cerevisiae12415 Cytoplasmic 12417 1 142 NUE_OEX_1 YMR209C S. cerevisiae 12421Cytoplasmic 12423, 12425, 12427, 12429 1 143 NUE_OEX_1 YMR233W S.cerevisiae 12441 Cytoplasmic 12443, 12445, 12447, 12449, 12451, 12453,12455, 12457, 12459, 12461, 12463, 12465 1 144 NUE_OEX_1 YMR278W S.cerevisiae 12471 Cytoplasmic 12473, 12475, 12477, 12479, 12481, 12483,12485, 12487, 12489, 12491, 12493, 12495, 12497, 12499, 12501, 12503,12505, 12507, 12509, 12511, 12513, 12515, 12517, 12519, 12521, 12523,12525, 12527, 12529, 12531, 12533, 12535, 12537, 12539, 12541, 12543,12545, 12547, 12549, 12551, 12553, 12555, 12557, 12559, 12561, 12563,12565, 12567, 12569, 12571, 12573, 12575, 12577, 12579, 12581, 12583,12585, 12587, 12589, 12591, 12593, 12595, 12597, 12599, 12601, 12603,12605, 12607, 12609, 12611, 12613, 12615, 12617, 12619, 12621, 12623,12625, 12627, 12629, 12631, 12633, 12635, 12637, 12639, 12641, 12643,12645, 12647, 12649, 12651, 12653, 12655, 12657, 12659, 12661, 12663,12665, 12667, 12669, 12671, 12673, 12675, 12677, 12679, 12681, 12683,12685, 12687, 12689, 12691, 12693, 12695, 12697, 12699, 12701, 12703,12705, 12707, 12709, 12711, 12713, 12715, 12717, 12719, 12721, 12723,12725, 12727, 12729, 12731, 12733, 12735, 12737, 12739 1 145 NUE_OEX_1YMR280C S. cerevisiae 12750 Cytoplasmic 12752, 12754, 12756 1 146NUE_OEX_1 YNL014W S. cerevisiae 12774 Cytoplasmic 12776, 12778, 12780,12782, 12784, 12786, 12788, 12790, 12792, 12794, 12796, 12798, 12800,12802, 12804, 12806, 12808, 12810 1 147 NUE_OEX_1 YNL320W S. cerevisiae12830 Cytoplasmic 12832, 12834, 12836, 12838, 12840, 12842, 12844,12846, 12848, 12850, 12852, 12854, 12856, 12858, 12860, 12862, 12864,12866 1 148 NUE_OEX_1 YOL007C S. cerevisiae 12884 Cytoplasmic 12886 1149 NUE_OEX_1 YOL164W S. cerevisiae 12890 Cytoplasmic 12892, 12894,12896, 12898, 12900, 12902, 12904, 12906, 12908, 12910, 12912, 12914,12916, 12918, 12920, 12922, 12924, 12926, 12928, 12930, 12932, 12934,12936, 12938, 12940, 12942, 12944, 12946, 12948, 12950, 12952, 12954,12956, 12958, 12960, 12962, 12964, 12966, 12968, 12970, 12972, 12974,12976, 12978, 12980, 12982, 12984, 12986, 12988, 12990, 12992, 12994,12996, 12998, 13000 1 150 NUE_OEX_1 YOR076C S. cerevisiae 13015Cytoplasmic — 1 151 NUE_OEX_1 YOR083W S. cerevisiae 13019 Cytoplasmic13021 1 152 NUE_OEX_1 YOR097C S. cerevisiae 13025 Cytoplasmic 13027 1153 NUE_OEX_1 YOR128C S. cerevisiae 13031 Cytoplasmic 13033, 13035,13037, 13039, 13041, 13043, 13045, 13047, 13049, 13051, 13053, 13055,13057, 13059, 13061, 13063, 13065, 13067, 13069, 13071, 13073, 13075,13077, 13079, 13081, 13083, 13085, 13087, 13089, 13091, 13093, 13095,13097 1 154 NUE_OEX_1 YOR353C S. cerevisiae 14086 Cytoplasmic 14088,14090 1 155 NUE_OEX_1 YPL141C S. cerevisiae 14094 Cytoplasmic 14096,14098, 14100 1 156 NUE_OEX_1 YPR088C S. cerevisiae 14114 Cytoplasmic14116, 14118, 14120, 14122, 14124, 14126, 14128, 14130, 14132, 14134,14136, 14138, 14140, 14142, 14144, 14146, 14148, 14150, 14152, 14154,14156, 14158, 14160, 14162, 14164, 14166, 14168, 14170, 14172, 14174,14176, 14178, 14180, 14182, 14184, 14186, 14188, 14190, 14192, 14194,14196, 14198, 14200, 14202, 14204, 14206, 14208, 14210, 14212, 14214 1157 NUE_OEX_1 YPR108W S. cerevisiae 14247 Cytoplasmic 14249, 14251,14253, 14255, 14257, 14259, 14261, 14263, 14265, 14267, 14269, 14271,14273, 14275, 14277, 14279, 14281, 14283, 14285, 14287, 14289 1 158NUE_OEX_1 YPR110C S. cerevisiae 14312 Cytoplasmic 14314, 14316, 14318,14320, 14322, 14324, 14326, 14328, 14330, 14332, 14334, 14336, 14338,14340, 14342, 14344, 14346, 14348, 14350, 14352, 14354, 14356, 14358,14360, 14362, 14364, 14366, 14368, 14370, 14372 1 159 NUE_OEX_1 B3825_2E. coli 14915 Plastidic 14917, 14919, 14921, 14923, 14925, 14927, 14929,14931, 14933, 14935, 14937, 14939, 14941, 14943, 14945, 14947, 14949,14951, 14953, 14955, 14957, 14959, 14961, 14963, 14965, 14967, 14969,14971, 14973, 14975, 14977, 14979, 14981, 14983, 14985, 14987, 14989,14991, 14993, 14995, 14997, 14999, 15001, 15003, 15005, 15007, 15009 1160 NUE_OEX_1 YIR034C_2 S. cerevisiae 15383 Cytoplasmic 15385, 15387,15389, 15391, 15393, 15395, 15397, 15399, 15401, 15403, 15405, 15407,15409, 15411, 15413, 15415, 15417, 15419 1 161 NUE_OEX_1 YJR131W_2 S.cerevisiae 15461 Cytoplasmic 15463, 15465, 15467, 15469, 15471, 15473,15475, 15477, 15479, 15481, 15483, 15485, 15487, 15489, 15491, 15493,15495, 15497, 15499, 15501, 15503, 15505, 15507, 15509, 15511, 15513,15515, 15517, 15519, 15521, 15523, 15525, 15527, 15529, 15531, 15533,15535, 15537, 15539, 15541, 15543, 15545, 15547, 15549, 15551, 15553,15555 1 162 NUE_OEX_1 YKL100C_2 S. cerevisiae 15572 Cytoplasmic 15574,15576, 15578, 15580 1 163 NUE_OEX_1 YKL193C_2 S. cerevisiae 15594Cytoplasmic 15596, 15598, 15600, 15602, 15604, 15606, 15608, 15610,15612, 15614, 15616, 15618, 15620, 15622, 15624, 15626, 15628, 15630 1164 NUE_OEX_1 YLL016W_2 S. cerevisiae 15647 Cytoplasmic 15649, 15651,15653, 15655, 15657, 15659, 15661 1 165 NUE_OEX_1 YLR034C_2 S.cerevisiae 15674 Cytoplasmic 15676, 15678, 15680, 15682, 15684, 15686,15688, 15690, 15692, 15694, 15696, 15698, 15700, 15702, 15704, 15706,15708, 15710, 15712, 15714, 15716, 15718, 15720, 15722, 15724, 15726,15728, 15730, 15732, 15734, 15736, 15738, 15740, 15742, 15744, 15746,15748, 15750, 15752, 15754, 15756, 15758, 15760, 15762, 15764, 15766,15768, 15770, 15772, 15774, 15776, 15778, 15780, 15782, 15784, 15786,15788, 15790, 15792, 15794, 15796, 15798, 15800, 15802, 15804, 15806,15808, 15810, 15812, 15814, 15816, 15818, 15820, 15822, 15824, 15826,15828, 15830, 15832, 15834, 15836, 15838, 15840, 15842, 15844, 15846,15848, 15850, 15852, 15854, 15856, 15858, 15860, 15862, 15864, 15866,15868, 15870, 15872, 15874, 15876, 15878, 15880, 15882, 15884, 15886,15888, 15890, 15892, 15894, 15896, 15898, 15900, 15902, 15904, 15906,15908, 15910, 15912, 15914, 15916, 15918, 15920, 15922, 15924, 15926,15928, 15930, 15932, 15934, 15936, 15938, 15940, 15942, 15944, 15946,15948, 15950, 15952, 15954, 15956, 15958, 15960, 15962, 15964, 15966,15968, 15970, 15972, 15974, 15976 1 166 NUE_OEX_1 YLR060W_2 S.cerevisiae 16006 Cytoplasmic 16008, 16010, 16012, 16014, 16016, 16018,16020, 16022, 16024, 16026, 16028, 16030, 16032, 16034, 16036, 16038,16040, 16042, 16044, 16046, 16048, 16050, 16052, 16054, 16056, 16058,16060, 16062, 16064, 16066, 16068, 16070, 16072, 16074, 16076, 16078,16080, 16082, 16084 1 167 NUE_OEX_1 YMR082C_2 S. cerevisiae 16115Cytoplasmic 16117 1 168 NUE_OEX_1 B1258 E. coli 14403 Cytoplasmic 14405,14407, 14409, 14411, 14413, 14415, 14417, 14419, 14421, 14423, 14425,14427, 14429, 14431, 14433, 14435, 14437, 14439, 14441, 14443, 14445,14447, 14449, 14451, 14453, 14455, 14457, 14459, 14461, 14463, 14465,14467, 14469, 14471, 14473, 14475, 14477, 14479, 14481, 14483, 14485,14487, 14489, 14491 1 169 NUE_OEX_1 YML101C S. cerevisiae 16094Cytoplasmic 16096, 16098, 16100 1 170 NUE_OEX_1 YMR065W S. cerevisiae16107 Cytoplasmic 16109, 16111 1 171 NUE_OEX_1 YMR163C S. cerevisiae16121 Cytoplasmic 16123, 16125, 16127 1 172 NUE_OEX_1 YOL042W S.cerevisiae 16276 Cytoplasmic 16278, 16280, 16282, 16284, 16286, 16288 1173 NUE_OEX_1 YOR226C S. cerevisiae 16306 Cytoplasmic 16308, 16310,16312, 16314, 16316, 16318, 16320, 16322, 16324, 16326, 16328, 16330,16332, 16334, 16336, 16338, 16340, 16342, 16344, 16346, 16348, 16350,16352, 16354, 16356, 16358, 16360, 16362, 16364, 16366, 16368, 16370,16372, 16374, 16376, 16378, 16380, 16382, 16384, 16386, 16388, 16390,16392, 16394, 16396, 16398, 16400, 16402, 16404, 16406, 16408, 16410,16412, 16414, 16416, 16418, 16420, 16422, 16424, 16426, 16428, 16430,16432, 16434, 16436, 16438, 16440, 16442, 16444, 16446, 16448, 16450,16452, 16454, 16456, 16458, 16460, 16462, 16464, 16466, 16468, 16470,16472, 16474, 16476, 16478, 16480, 16482, 16484, 16486, 16488, 16490,16492, 16494, 16496, 16498, 16500, 16502, 16504, 16506, 16508, 16510,16512, 16514, 16516, 16518, 16520, 16522, 16524, 16526, 16528, 16530,16532, 16534, 16536 1 174 NUE_OEX_1 YPL068C S. cerevisiae 16574Cytoplasmic 16576, 16578 1 175 NUE_OEX_1 B0165 E. coli 14397 Plastidic14399 1 176 NUE_OEX_1 YOR203W S. cerevisiae 16300 Cytoplasmic 16302 1177 NUE_OEX_1 YNL147W S. cerevisiae 16134 Cytoplasmic 16136, 16138,16140, 16142, 16144, 16146, 16148, 16150, 16152, 16154, 16156, 16158,16160, 16162, 16164, 16166, 16168, 16170, 16172, 16174, 16176, 16178,16180, 16182, 16184, 16186, 16188, 16190, 16192, 16194, 16196, 16198,16200, 16202, 16204, 16206, 16208, 16210, 16212, 16214, 16216, 16218,16220, 16222, 16224, 16226, 16228, 16230, 16232, 16234, 16236, 16238,16240, 16242, 16244, 16246, 16248, 16250, 16252, 16254, 16256 1 178NUE_OEX_1 YBR083W S. cerevisiae 15057 Cytoplasmic 15059, 15061 1 179NUE_OEX_1 YKL111C S. cerevisiae 15588 Cytoplasmic 15590 1 180 NUE_OEX_1YPR067W S. cerevisiae 16583 Cytoplasmic 16585, 16587, 16589, 16591,16593, 16595, 16597, 16599, 16601, 16603, 16605, 16607, 16609, 16611,16613, 16615, 16617, 16619, 16621, 16623 1 181 NUE_OEX_1 B1985 E. coli14840 Cytoplasmic 14842, 14844, 14846, 14848, 14850, 14852, 14854,14856, 14858, 14860, 14862, 14864, 14866 1 182 NUE_OEX_1 B3838 E. coli15015 Cytoplasmic 15017, 15019, 15021, 15023, 15025, 15027, 15029,15031, 15033, 15035, 15037, 15039, 15041, 15043, 15045, 15047, 15049 1183 NUE_OEX_1 YJL010C S. cerevisiae 15433 Cytoplasmic 15435, 15437,15439, 15441, 15443, 15445, 15447, 15449 1 184 NUE_OEX_1 B1267 E. coli14498 Cytoplasmic 14500, 14502, 14504, 14506, 14508, 14510, 14512,14514, 14516, 14518, 14520, 14522, 14524, 14526, 14528, 14530, 14532,14534, 14536, 14538, 14540, 14542, 14544, 14546, 14548, 14550, 14552,14554, 14556, 14558, 14560, 14562, 14564, 14566, 14568, 14570, 14572,14574, 14576, 14578, 14580, 14582, 14584, 14586, 14588, 14590, 14592,14594, 14596, 14598, 14600, 14602, 14604, 14606, 14608, 14610, 14612,14614, 14616, 14618, 14620, 14622, 14624, 14626, 14628, 14630, 14632,14634, 14636, 14638, 14640, 14642, 14644, 14646, 14648, 14650, 14652,14654, 14656, 14658, 14660, 14662, 14664, 14666, 14668, 14670, 14672,14674, 14676, 14678, 14680, 14682, 14684, 14686, 14688, 14690, 14692,14694, 14696, 14698, 14700, 14702, 14704, 14706, 14708 1 185 NUE_OEX_1B1322 E. coli 14719 Cytoplasmic 14721, 14723, 14725, 14727, 14729,14731, 14733, 14735, 14737, 14739, 14741, 14743, 14745, 14747, 14749,14751, 14753, 14755, 14757, 14759, 14761, 14763, 14765, 14767, 14769,14771, 14773, 14775, 14777, 14779, 14781, 14783, 14785 1 186 NUE_OEX_1B1381 E. coli 14792 Cytoplasmic 14794, 14796, 14798, 14800, 14802,14804, 14806, 14808, 14810, 14812, 14814, 14816, 14818, 14820 1 187NUE_OEX_1 B2646 E. coli 14880 Cytoplasmic 14882, 14884, 14886, 14888,14890, 14892, 14894, 14896, 14898, 14900, 14902, 14904, 14906, 14908 1188 NUE_OEX_1 YBR191W S. cerevisiae 15065 Cytoplasmic 15067, 15069,15071, 15073, 15075, 15077, 15079, 15081, 15083, 15085, 15087, 15089,15091, 15093, 15095, 15097, 15099, 15101, 15103, 15105, 15107, 15109,15111, 15113, 15115, 15117, 15119, 15121, 15123, 15125, 15127, 15129,15131, 15133, 15135, 15137, 15139, 15141, 15143, 15145, 15147, 15149,15151, 15153, 15155, 15157, 15159, 15161, 15163, 15165, 15167, 15169,15171, 15173, 15175, 15177, 15179, 15181, 15183, 15185, 15187, 15189,15191, 15193, 15195, 15197, 15199, 15201, 15203, 15205, 15207, 15209,15211, 15213, 15215, 15217 1 189 NUE_OEX_1 YDL135C S. cerevisiae 15258Cytoplasmic 15260, 15262, 15264, 15266, 15268, 15270, 15272, 15274,15276, 15278, 15280, 15282, 15284, 15286, 15288, 15290, 15292, 15294,15296, 15298, 15300, 15302, 15304, 15306, 15308, 15310, 15312, 15314,15316, 15318, 15320, 15322, 15324, 15326, 15328, 15330, 15332, 15334,15336, 15338, 15340, 15342, 15344, 15346, 15348, 15350, 15352, 15354,15356 1 190 NUE_OEX_1 YHL005C S. cerevisiae 15379 Cytoplasmic — 1 191NUE_OEX_1 YKR100C_2 S. cerevisiae 16630 Cytoplasmic 16632, 16634, 16636,16638 1 192 NUE_OEX_1 YMR191W_2 S. cerevisiae 16648 Cytoplasmic 16650,16652

TABLE IIA_CHOM Amino acid sequence ID numbers 5. 1. 2. 3. 4. Lead 6. 7.Application Hit Project Locus Organism SEQ ID Target SEQ IDs ofPolypeptide Homologs 1 1 NUE_OE yor128c S. 13031 Cytoplasmic 13118,13120, 13122, 13124, 13126, 13128, 13130, 13132, X_1 CHOM cerevisiae13134, 13136, 13138, 13140, 13142, 13144, 13146, 13148, 13150, 13152,13154, 13156, 13158, 13160, 13162, 13164, 13166, 13168, 13170, 13172,13174, 13176, 13178, 13180, 13182, 13184, 13186, 13188, 13190, 13192,13194, 13196, 13198, 13200, 13202, 13204, 13206, 13208, 13210, 13212,13214, 13216, 13218, 13220, 13222, 13224, 13226, 13228, 13230, 13232,13234, 13236, 13238, 13240, 13242, 13244, 13246, 13248, 13250, 13252,13254, 13256, 13258, 13260, 13262, 13264, 13266, 13268, 13270, 13272,13274, 13276, 13278, 13280, 13282, 13284, 13286, 13288, 13290, 13292,13294, 13296, 13298, 13300, 13302, 13304, 13306, 13308, 13310, 13312,13314, 13316, 13318, 13320, 13322, 13324, 13326, 13328, 13330, 13332,13334, 13336, 13338, 13340, 13342, 13344, 13346, 13348, 13350, 13352,13354, 13356, 13358, 13360, 13362, 13364, 13366, 13368, 13370, 13372,13374, 13376, 13378, 13380, 13382, 13384, 13386, 13388, 13390, 13392,13394, 13396, 13398, 13400, 13402, 13404, 13406, 13408, 13410, 13412,13414, 13416, 13418, 13420, 13422, 13424, 13426, 13428, 13430, 13432,13434, 13436, 13438, 13440, 13442, 13444, 13446, 13448, 13450, 13452,13454, 13456, 13458, 13460, 13462, 13464, 13466, 13468, 13470, 13472,13474, 13476, 13478, 13480, 13482, 13484, 13486, 13488, 13490, 13492,13494, 13496, 13498, 13500, 13502, 13504, 13506, 13508, 13510, 13512,13514, 13516, 13518, 13520, 13522, 13524, 13526, 13528, 13530, 13532,13534, 13536, 13538, 13540, 13542, 13544, 13546, 13548, 13550, 13552,13554, 13556, 13558, 13560, 13562, 13564, 13566, 13568, 13570, 13572,13574, 13576, 13578, 13580, 13582, 13584, 13586, 13588, 13590, 13592,13594, 13596, 13598, 13600, 13602, 13604, 13606, 13608, 13610, 13612,13614, 13616

TABLE IIA_NHOM Amino acid sequence ID numbers 5. 1. 2. 3. 4. Lead 6. 7.Application Hit Project Locus Organism SEQ ID Target SEQ IDs ofPolypeptide Homologs 1 1 NUE_OE yor128c S. 13031 Cytoplasmic 13625,13627, 13629, 13631, 13633, 13635, 13637, 13639, X_1 NHOM cerevisiae13641, 13643, 13645, 13647, 13649, 13651, 13653, 13655, 13657, 13659,13661, 13663, 13665, 13667, 13669, 13671, 13673, 13675, 13677, 13679,13681, 13683, 13685, 13687, 13689, 13691, 13693, 13695, 13697, 13699,13701, 13703, 13705, 13707, 13709, 13711, 13713, 13715, 13717, 13719,13721, 13723, 13725, 13727, 13729, 13731, 13733, 13735, 13737, 13739,13741, 13743, 13745, 13747, 13749, 13751, 13753, 13755, 13757, 13759,13761, 13763, 13765, 13767, 13769, 13771, 13773, 13775, 13777, 13779,13781, 13783, 13785, 13787, 13789, 13791, 13793, 13795, 13797, 13799,13801, 13803, 13805, 13807, 13809, 13811, 13813, 13815, 13817, 13819,13821, 13823, 13825, 13827, 13829, 13831, 13833, 13835, 13837, 13839,13841, 13843, 13845, 13847, 13849, 13851, 13853, 13855, 13857, 13859,13861, 13863, 13865, 13867, 13869, 13871, 13873, 13875, 13877, 13879,13881, 13883, 13885, 13887, 13889, 13891, 13893, 13895, 13897, 13899,13901, 13903, 13905, 13907, 13909, 13911, 13913, 13915, 13917, 13919,13921, 13923, 13925, 13927, 13929, 13931, 13933, 13935, 13937, 13939,13941, 13943, 13945, 13947, 13949, 13951, 13953, 13955, 13957, 13959,13961, 13963, 13965, 13967, 13969, 13971, 13973, 13975, 13977, 13979,13981, 13983, 13985, 13987, 13989, 13991, 13993, 13995, 13997, 13999,14001, 14003, 14005, 14007, 14009, 14011, 14013, 14015, 14017, 14019,14021, 14023, 14025, 14027, 14029, 14031, 14033, 14035, 14037, 14039,14041, 14043, 14045, 14047, 14049, 14051, 14053, 14055, 14057, 14059,14061, 14063, 14065, 14067, 14069, 14071, 14073, 14075, 14077, 14079,14081

TABLE IIB Amino acid sequence ID numbers 5. 1. 2. 3. 4. Lead 6. 7.Application Hit Project Locus Organism SEQ ID Target SEQ IDs ofPolypeptide Homologs 1 1 NUE_OE B0017 E. coli 39 Cytoplasmic — X_1 1 2NUE_OE B0045 E. coli 43 Cytoplasmic 99, 101, 103, 105, 107, 109, 111,113, 115, 117 X_1 1 3 NUE_OE B0180 E. coli 124 Plastidic 366, 368, 370,372, 374 X_1 1 4 NUE_OE B0242 E. coli 381 Plastidic 663, 665, 667, 669X_1 1 5 NUE_OE B0403 E. coli 680 Plastidic — X_1 1 6 NUE_OE B0474 E.coli 813 Cytoplasmic 959, 961, 963, 965, 967, 969, 971, 973, 975, 977,X_1 979, 981, 983, 985, 987, 989, 991, 993, 995, 997, 999, 1001, 1003,1005, 1007, 1009, 1011, 1013, 1015, 1017, 1019, 1021, 1023, 1025, 1027,1029, 1031, 1033, 1035, 1037, 1039, 1041, 1043, 1045, 1047, 1049, 166581 7 NUE_OE B0754 E. coli 1056 Plastidic — X_1 1 8 NUE_OE B0784 E. coli1564 Cytoplasmic — X_1 1 9 NUE_OE B0873 E. coli 1706 Plastidic — X_1 110 NUE_OE B1014 E. coli 1845 Cytoplasmic — X_1 1 11 NUE_OE B1020 E. coli1951 Plastidic — X_1 1 12 NUE_OE B1180 E. coli 1976 Cytoplasmic 2100,2102, 2104, 2106, 2108, 2110, 2112, 2114, X_1 2116, 2118, 2120, 16662 113 NUE_OE B1933 E. coli 2128 Plastidic — X_1 1 14 NUE_OE B2032 E. coli2136 Plastidic — X_1 1 15 NUE_OE B2165 E. coli 2172 Plastidic 2286, 2288X_1 1 16 NUE_OE B2223 E. coli 2298 Plastidic — X_1 1 17 NUE_OE B2238 E.coli 2427 Plastidic — X_1 1 17 NUE_OE B2238 E. coli 2427 Cytoplasmic —X_1 1 18 NUE_OE B2310 E. coli 2453 Plastidic — X_1 1 19 NUE_OE B2431 E.coli 2552 Plastidic — X_1 1 20 NUE_OE B2600 E. coli 2601 Plastidic — X_11 21 NUE_OE B2766 E. coli 2669 Plastidic — X_1 1 22 NUE_OE B2903 E. coli2773 Cytoplasmic 3097, 3099 X_1 1 23 NUE_OE B3117 E. coli 3118 Plastidic3374, 3376, 3378, 3380, 3382 X_1 1 24 NUE_OE B3120 E. coli 3391Plastidic — X_1 1 25 NUE_OE B3216 E. coli 3397 Plastidic — X_1 1 26NUE_OE B3451 E. coli 3471 Plastidic — X_1 1 27 NUE_OE B3791 E. coli 3564Cytoplasmic — X_1 1 28 NUE_OE B3825 E. coli 3771 Plastidic — X_1 1 29NUE_OE YAL019W S. 3869 Cytoplasmic — X_1 cerevisiae 1 30 NUE_OE YAR035WS. 3896 Cytoplasmic — X_1 cerevisiae 1 31 NUE_OE YBL021C S. 3954Cytoplasmic 4032, 4034, 4036, 4038, 4040, 4042, 4044, 4046, X_1cerevisiae 4048, 4050, 4052, 4054, 4056, 4058, 4060, 4062, 4064, 4066,4068, 4070, 4072, 4074, 4076, 4078, 4080, 4082, 4084, 4086, 4088, 4090,4092, 4094, 4096, 4098, 4100, 4102, 4104, 4106 1 32 NUE_OE YBR055C S.4112 Cytoplasmic — X_1 cerevisiae 1 33 NUE_OE YBR128C S. 4150Cytoplasmic — X_1 cerevisiae 1 34 NUE_OE YBR159W S. 4163 Cytoplasmic4215, 4217, 4219, 4221, 4223, 4225, 4227 X_1 cerevisiae 1 35 NUE_OEYBR243C S. 4236 Cytoplasmic 4268, 4270 X_1 cerevisiae 1 35 NUE_OEYBR243C S. 4236 Plastidic 4268, 4270 X_1 cerevisiae 1 36 NUE_OE YBR262CS. 4281 Cytoplasmic — X_1 cerevisiae 1 37 NUE_OE YCR019W S. 4289Cytoplasmic — X_1 cerevisiae 1 38 NUE_OE YDR070C S. 4316 Cytoplasmic —X_1 cerevisiae 1 39 NUE_OE YDR079W S. 4326 Cytoplasmic — X_1 cerevisiae1 40 NUE_OE YDR123C S. 4336 Cytoplasmic — X_1 cerevisiae 1 41 NUE_OEYDR137W S. 4347 Cytoplasmic — X_1 cerevisiae 1 42 NUE_OE YDR294C S. 4362Cytoplasmic — X_1 cerevisiae 1 42 NUE_OE YDR294C S. 4362 Plastidic — X_1cerevisiae 1 43 NUE_OE YDR330W S. 4403 Cytoplasmic — X_1 cerevisiae 1 44NUE_OE YDR355C S. 4432 Cytoplasmic — X_1 cerevisiae 1 45 NUE_OE YDR430CS. 4436 Plastidic — X_1 cerevisiae 1 46 NUE_OE YDR472W S. 4486Cytoplasmic — X_1 cerevisiae 1 47 NUE_OE YDR497C S. 4507 Plastidic 4739,4741, 4743, 4745, 4747, 4749, 4751, 4753, X_1 cerevisiae 4755, 4757,4759, 4761, 4763, 4765, 4767, 4769, 4771, 4773, 4775, 4777, 4779, 4781,4783, 4785, 16666 1 48 NUE_OE YER029C S. 4791 Cytoplasmic — X_1cerevisiae 1 49 NUE_OE YFR007W S. 4807 Cytoplasmic — X_1 cerevisiae 1 50NUE_OE YGL039W S. 4837 Cytoplasmic 5215, 5217, 5219, 5221, 5223, 5225,5227, 5229, X_1 cerevisiae 5231, 5233, 5235, 5237, 5239, 5241, 5243,5245, 5247, 5249, 5251, 5253, 5255, 5257, 5259, 5261, 5263, 5265, 5267,5269, 5271, 5273, 5275, 5277, 5279, 5281, 5283, 5285, 5287, 5289, 5291,5293, 5295, 5297, 5299, 5301, 5303, 5305 1 51 NUE_OE YGL043W S. 5312Cytoplasmic 5336, 5338, 5340 X_1 cerevisiae 1 52 NUE_OE YGR088W S. 5347Cytoplasmic 5525 X_1 cerevisiae 1 53 NUE_OE YGR122C-A S. 5534Cytoplasmic — X_1 cerevisiae 1 54 NUE_OE YGR142W S. 5552 Cytoplasmic —X_1 cerevisiae 1 55 NUE_OE YGR143W S. 5560 Cytoplasmic — X_1 cerevisiae1 56 NUE_OE YGR165W S. 5603 Cytoplasmic — X_1 cerevisiae 1 57 NUE_OEYGR170W S. 5609 Cytoplasmic — X_1 cerevisiae 1 58 NUE_OE YGR202C S. 5615Cytoplasmic — X_1 cerevisiae 1 59 NUE_OE YGR266W S. 5667 Cytoplasmic —X_1 cerevisiae 1 60 NUE_OE YGR282C S. 5702 Cytoplasmic — X_1 cerevisiae1 61 NUE_OE YGR290W S. 5751 Cytoplasmic — X_1 cerevisiae 1 62 NUE_OEYHL021C S. 5755 Cytoplasmic — X_1 cerevisiae 1 63 NUE_OE YHL031C S. 5779Cytoplasmic — X_1 cerevisiae 1 64 NUE_OE YHR011W S. 5813 Cytoplasmic5955, 5957, 5959, 16670 X_1 cerevisiae 1 65 NUE_OE YHR127W S. 5968Cytoplasmic — X_1 cerevisiae 1 66 NUE_OE YHR137W S. 5974 Cytoplasmic —X_1 cerevisiae 1 66 NUE_OE YHR137W S. 5974 Plastidic — X_1 cerevisiae 167 NUE_OE YIL099W S. 6028 Cytoplasmic — X_1 cerevisiae 1 67 NUE_OEYIL099W S. 6028 Plastidic — X_1 cerevisiae 1 68 NUE_OE YIL147C S. 6108Cytoplasmic — X_1 cerevisiae 1 69 NUE_OE YIR034C S. 6151 Cytoplasmic —X_1 cerevisiae 1 70 NUE_OE YJL013C S. 6199 Cytoplasmic — X_1 cerevisiae1 71 NUE_OE YJL041W S. 6209 Cytoplasmic — X_1 cerevisiae 1 72 NUE_OEYJL064W S. 6243 Cytoplasmic — X_1 cerevisiae 1 73 NUE_OE YJL067W S. 6247Cytoplasmic — X_1 cerevisiae 1 74 NUE_OE YJL094C S. 6251 Cytoplasmic —X_1 cerevisiae 1 75 NUE_OE YJL171C S. 6298 Cytoplasmic — X_1 cerevisiae1 76 NUE_OE YJL213W S. 6327 Cytoplasmic — X_1 cerevisiae 1 77 NUE_OEYJR017C S. 6489 Cytoplasmic 6543 X_1 cerevisiae 1 78 NUE_OE YJR058C S.6551 Cytoplasmic 6663, 6665, 6667, 6669, 6671, 6673, 6675, 6677, X_1cerevisiae 6679, 6681, 6683, 6685, 6687, 6689, 6691, 6693, 6695, 16674,16676 1 79 NUE_OE YJR117W S. 6701 Cytoplasmic 6791, 6793, 6795, 6797,6799, 6801, 6803, 6805, X_1 cerevisiae 6807 1 80 NUE_OE YJR121W S. 6817Cytoplasmic 7337, 7339, 7341, 7343, 7345, 7347, 7349 X_1 cerevisiae 1 81NUE_OE YJR131W S. 7367 Cytoplasmic 7461, 7463, 7465, 7467 X_1 cerevisiae1 82 NUE_OE YJR145C S. 7476 Cytoplasmic 7560, 7562, 7564, 7566, 7568,7570, 7572, 7574, X_1 cerevisiae 7576, 7578, 7580, 7582, 7584, 7586,7588, 7590, 7592, 7594, 7596, 16680 1 83 NUE_OE YKL084W S. 7603Cytoplasmic — X_1 cerevisiae 1 84 NUE_OE YKL088W S. 7652 Cytoplasmic —X_1 cerevisiae 1 85 NUE_OE YKL100C S. 7662 Cytoplasmic — X_1 cerevisiae1 86 NUE_OE YKL131W S. 7676 Cytoplasmic — X_1 cerevisiae 1 87 NUE_OEYKL138C S. 7680 Cytoplasmic — X_1 cerevisiae 1 88 NUE_OE YKL178C S. 7711Cytoplasmic — X_1 cerevisiae 1 89 NUE_OE YKL179C S. 7736 Cytoplasmic —X_1 cerevisiae 1 90 NUE_OE YKL193C S. 7779 Cytoplasmic 7815, 7817, 7819,7821 X_1 cerevisiae 1 91 NUE_OE YKL216W S. 7830 Cytoplasmic — X_1cerevisiae 1 92 NUE_OE YKR016W S. 8018 Cytoplasmic — X_1 cerevisiae 1 93NUE_OE YKR021W S. 8046 Cytoplasmic — X_1 cerevisiae 1 94 NUE_OE YKR055WS. 8074 Cytoplasmic 8258 X_1 cerevisiae 1 95 NUE_OE YKR088C S. 8264Plastidic — X_1 cerevisiae 1 96 NUE_OE YKR093W S. 8288 Cytoplasmic 8444,8446, 8448, 8450, 8452, 8454, 8456, 8458, X_1 cerevisiae 8460, 8462 1 97NUE_OE YKR099W S. 8469 Cytoplasmic — X_1 cerevisiae 1 98 NUE_OE YKR100CS. 8485 Cytoplasmic — X_1 cerevisiae 1 99 NUE_OE YLL014W S. 8493Cytoplasmic — X_1 cerevisiae 1 100 NUE_OE YLL016W S. 8515 Cytoplasmic —X_1 cerevisiae 1 101 NUE_OE YLL023C S. 8540 Cytoplasmic — X_1 cerevisiae1 102 NUE_OE YLL037W S. 8572 Cytoplasmic — X_1 cerevisiae 1 103 NUE_OEYLL049W S. 8576 Cytoplasmic — X_1 cerevisiae 1 104 NUE_OE YLL055W S.8580 Cytoplasmic — X_1 cerevisiae 1 105 NUE_OE YLR034C S. 8662Cytoplasmic 8964, 8966, 8968, 8970, 8972, 8974, 8976, 8978, X_1cerevisiae 8980, 8982 1 106 NUE_OE YLR042C S. 8992 Cytoplasmic — X_1cerevisiae 1 107 NUE_OE YLR053C S. 8996 Cytoplasmic — X_1 cerevisiae 1108 NUE_OE YLR058C S. 9000 Cytoplasmic 9502, 9504, 9506, 9508, 9510,9512, 9514, 9516, X_1 cerevisiae 9518, 9520, 9522, 9524, 9526, 9528,9530, 9532, 9534, 9536, 9538, 9540 1 109 NUE_OE YLR060W S. 9552Cytoplasmic — X_1 cerevisiae 1 110 NUE_OE YLR065C S. 9638 Cytoplasmic —X_1 cerevisiae 1 111 NUE_OE YLR070C S. 9673 Cytoplasmic 10119, 10121,10123, 10125, 10127, 10129, 10131, X_1 cerevisiae 10133, 10135, 10137,10139, 10141, 10143, 10145, 10147, 10149, 10151, 10153, 10155, 10157,10159, 10161, 10163, 10165, 10167, 10169, 10171, 10173, 10175, 10177 1112 NUE_OE YLR100W S. 10183 Cytoplasmic — X_1 cerevisiae 1 113 NUE_OEYLR109W S. 10215 Cytoplasmic 10419, 10421, 10423, 10425, 10427, 10429,10431, X_1 cerevisiae 10433, 10435, 10437, 10439, 10441, 10443 1 114NUE_OE YLR125W S. 10448 Cytoplasmic — X_1 cerevisiae 1 115 NUE_OEYLR127C S. 10452 Cytoplasmic — X_1 cerevisiae 1 116 NUE_OE YLR185W S.10464 Cytoplasmic 10514, 10516, 10518, 10520, 10522, 10524, 10526 X_1cerevisiae 1 117 NUE_OE YLR204W S. 10534 Cytoplasmic — X_1 cerevisiae 1117 NUE_OE YLR204W S. 10534 Plastidic — X_1 cerevisiae 1 118 NUE_OEYLR242C S. 10542 Cytoplasmic — X_1 cerevisiae 1 119 NUE_OE YLR293C S.10563 Cytoplasmic 10715, 10717, 10719, 10721, 10723, 10725, 10727, X_1cerevisiae 10729, 10731, 10733, 10735, 10737, 10739, 10741, 10743,10745, 10747, 10749, 10751, 10753, 10755, 10757, 10759, 10761, 10763,10765, 10767, 10769, 10771, 10773, 10775, 10777, 10779, 10781, 10783,10785, 10787, 10789, 10791, 10793, 10795, 10797, 10799, 10801, 10803,10805, 10807, 10809, 10811, 10813, 10815, 10817, 10819, 10821, 10823,10825, 10827, 10829, 10831, 10833, 10835, 10837, 10839, 10841, 10843,10845, 10847, 10849, 10851, 10853, 10855, 10857, 10859, 10861, 10863,10865, 10867, 10869, 10871, 10873, 10875, 10877, 10879, 10881, 10883,10885, 10887, 10889, 10891, 10893, 10895, 10899, 10901, 10903, 10897,10905, 10907, 10909, 10911, 10913, 10915, 10917, 10919, 10921, 10923,10925, 10927, 10929, 10931, 10933, 10935, 10937, 10939, 10941, 10943,10945, 10947, 10949, 10951, 10953, 10955, 10957, 10959, 10961, 10963,10965, 10967, 10969, 10971, 10973, 10975, 10977, 10979, 10981, 10983 1120 NUE_OE YLR313C S. 10991 Cytoplasmic — X_1 cerevisiae 1 121 NUE_OEYLR315W S. 10999 Cytoplasmic — X_1 cerevisiae 1 122 NUE_OE YLR329W S.11005 Cytoplasmic — X_1 cerevisiae 1 123 NUE_OE YLR362W S. 11013Cytoplasmic — X_1 cerevisiae 1 124 NUE_OE YLR395C S. 11055 Cytoplasmic —X_1 cerevisiae 1 125 NUE_OE YLR404W S. 11067 Cytoplasmic — X_1cerevisiae 1 126 NUE_OE YLR463C S. 11075 Cytoplasmic — X_1 cerevisiae 1127 NUE_OE YML022W S. 11081 Cytoplasmic 11527, 11529, 11531, 11533,11535, 11537, 11539, X_1 cerevisiae 11541, 11543, 11545, 11547 1 128NUE_OE YML027W S. 11553 Cytoplasmic — X_1 cerevisiae 1 129 NUE_OEYML065W S. 11570 Cytoplasmic — X_1 cerevisiae 1 130 NUE_OE YML089C S.11597 Cytoplasmic — X_1 cerevisiae 1 131 NUE_OE YML128C S. 11601Cytoplasmic — X_1 cerevisiae 1 132 NUE_OE YMR011W S. 11613 Cytoplasmic12125, 12127, 12129, 12131, 12133, 12135, 12137, X_1 cerevisiae 12139,12141, 12143, 12145, 12147, 12149, 12151, 12153, 12155, 12157, 12159,12161, 12163, 12165, 12167, 12169, 12171, 12173, 12175, 12177, 12179,12181, 12183, 12185, 12187, 12189, 12191, 12193, 12195, 12197, 12199,12201, 12203, 12205, 12207, 12209, 12211, 12213, 12215, 12217, 12219,12221, 12223, 12225, 12227, 12229, 12231, 12233, 12235, 12237, 12239,12241 1 133 NUE_OE YMR037C S. 12247 Cytoplasmic — X_1 cerevisiae 1 134NUE_OE YMR049C S. 12264 Cytoplasmic — X_1 cerevisiae 1 135 NUE_OEYMR052W S. 12317 Cytoplasmic — X_1 cerevisiae 1 136 NUE_OE YMR082C S.12328 Cytoplasmic — X_1 cerevisiae 1 137 NUE_OE YMR125W S. 12332Cytoplasmic — X_1 cerevisiae 1 138 NUE_OE YMR126C S. 12379 Cytoplasmic —X_1 cerevisiae 1 139 NUE_OE YMR144W S. 12395 Cytoplasmic — X_1cerevisiae 1 140 NUE_OE YMR160W S. 12407 Cytoplasmic — X_1 cerevisiae 1141 NUE_OE YMR191W S. 12415 Cytoplasmic — X_1 cerevisiae 1 142 NUE_OEYMR209C S. 12421 Cytoplasmic — X_1 cerevisiae 1 143 NUE_OE YMR233W S.12441 Cytoplasmic — X_1 cerevisiae 1 144 NUE_OE YMR278W S. 12471Cytoplasmic — X_1 cerevisiae 1 145 NUE_OE YMR280C S. 12750 Cytoplasmic —X_1 cerevisiae 1 146 NUE_OE YNL014W S. 12774 Cytoplasmic — X_1cerevisiae 1 147 NUE_OE YNL320W S. 12830 Cytoplasmic 12868, 12870,12872, 12874 X_1 cerevisiae 1 148 NUE_OE YOL007C S. 12884 Cytoplasmic —X_1 cerevisiae 1 149 NUE_OE YOL164W S. 12890 Cytoplasmic — X_1cerevisiae 1 150 NUE_OE YOR076C S. 13015 Cytoplasmic — X_1 cerevisiae 1151 NUE_OE YOR083W S. 13019 Cytoplasmic — X_1 cerevisiae 1 152 NUE_OEYOR097C S. 13025 Cytoplasmic — X_1 cerevisiae 1 153 NUE_OE YOR128C S.13031 Cytoplasmic 13099 X_1 cerevisiae 1 154 NUE_OE YOR353C S. 14086Cytoplasmic — X_1 cerevisiae 1 155 NUE_OE YPL141C S. 14094 Cytoplasmic —X_1 cerevisiae 1 156 NUE_OE YPR088C S. 14114 Cytoplasmic 14216, 14218,14220, 14222, 14224, 14226, 14228, X_1 cerevisiae 14230, 14232, 14234 1157 NUE_OE YPR108W S. 14247 Cytoplasmic 14291, 14293, 14295, 14297,14299 X_1 cerevisiae 1 158 NUE_OE YPR110C S. 14312 Cytoplasmic 14374,14376, 14378, 14380, 14382 X_1 cerevisiae 1 159 NUE_OE B3825_2 E. coli14915 Plastidic — X_1 1 160 NUE_OE YIR034C_2 S. 15383 Cytoplasmic — X_1cerevisiae 1 161 NUE_OE YJR131W_2 S. 15461 Cytoplasmic 15557, 15559,15561, 15563 X_1 cerevisiae 1 162 NUE_OE YKL100C_2 S. 15572 Cytoplasmic— X_1 cerevisiae 1 163 NUE_OE YKL193C_2 S. 15594 Cytoplasmic 15632,15634, 15636, 15638 X_1 cerevisiae 1 164 NUE_OE YLL016W_2 S. 15647Cytoplasmic — X_1 cerevisiae 1 165 NUE_OE YLR034C_2 S. 15674 Cytoplasmic15978, 15980, 15982, 15984, 15986, 15988, 15990, X_1 cerevisiae 15992,15994, 15996 1 166 NUE_OE YLR060W_2 S. 16006 Cytoplasmic — X_1cerevisiae 1 167 NUE_OE YMR082C_2 S. 16115 Cytoplasmic — X_1 cerevisiae1 168 NUE_OE B1258 E. coli 14403 Cytoplasmic — X_1 1 169 NUE_OE YML101CS. 16094 Cytoplasmic — X_1 cerevisiae 1 170 NUE_OE YMR065W S. 16107Cytoplasmic — X_1 cerevisiae 1 171 NUE_OE YMR163C S. 16121 Cytoplasmic —X_1 cerevisiae 1 172 NUE_OE YOL042W S. 16276 Cytoplasmic — X_1cerevisiae 1 173 NUE_OE YOR226C S. 16306 Cytoplasmic 16538, 16540,16542, 16544, 16546, 16548, 16550, X_1 cerevisiae 16552, 16554, 16556,16558, 16560, 16562, 16564, 16566 1 174 NUE_OE YPL068C S. 16574Cytoplasmic — X_1 cerevisiae 1 175 NUE_OE B0165 E. coli 14397 Plastidic— X_1 1 176 NUE_OE YOR203W S. 16300 Cytoplasmic — X_1 cerevisiae 1 177NUE_OE YNL147W S. 16134 Cytoplasmic 16258, 16260, 16262, 16264, 16266,16268, 16270 X_1 cerevisiae 1 178 NUE_OE YBR083W S. 15057 Cytoplasmic —X_1 cerevisiae 1 179 NUE_OE YKL111C S. 15588 Cytoplasmic — X_1cerevisiae 1 180 NUE_OE YPR067W S. 16583 Cytoplasmic — X_1 cerevisiae 1181 NUE_OE B1985 E. coli 14840 Cytoplasmic — X_1 1 182 NUE_OE B3838 E.coli 15015 Cytoplasmic — X_1 1 183 NUE_OE YJL010C S. 15433 Cytoplasmic —X_1 cerevisiae 1 184 NUE_OE B1267 E. coli 14498 Cytoplasmic 14710, 14712X_1 1 185 NUE_OE B1322 E. coli 14719 Cytoplasmic — X_1 1 186 NUE_OEB1381 E. coli 14792 Cytoplasmic — X_1 1 187 NUE_OE B2646 E. coli 14880Cytoplasmic — X_1 1 188 NUE_OE YBR191W S. 15065 Cytoplasmic 15219,15221, 15223, 15225, 15227, 15229, 15231, X_1 cerevisiae 15233, 15235,15237, 15239, 15241, 15243, 15245, 15247, 15249 1 189 NUE_OE YDL135C S.15258 Cytoplasmic 15358, 15360, 15362, 15364, 15366, 15368, 15370, X_1cerevisiae 15372 1 190 NUE_OE YHL005C S. 15379 Cytoplasmic — X_1cerevisiae 1 191 NUE_OE YKR100C_2 S. 16630 Cytoplasmic — X_1 cerevisiae1 192 NUE_OE YMR191W_2 S. 16648 Cytoplasmic — X_1 cerevisiae

TABLE III Primer nucleic acid sequence ID numbers 5. 1. 2. 3. 4. Lead 6.7. Application Hit Project Locus Organism SEQ ID Target SEQ IDs ofPrimers 1 1 NUE_OE B0017 E. coli 38 Cytoplasmic 40, 41 X_1 1 2 NUE_OEB0045 E. coli 42 Cytoplasmic 118, 119 X_1 1 3 NUE_OE B0180 E. coli 123Plastidic 375, 376 X_1 1 4 NUE_OE B0242 E. coli 380 Plastidic 670, 671X_1 1 5 NUE_OE B0403 E. coli 679 Plastidic 801, 802 X_1 1 6 NUE_OE B0474E. coli 812 Cytoplasmic 1050, 1051 X_1 1 7 NUE_OE B0754 E. coli 1055Plastidic 1551, 1552 X_1 1 8 NUE_OE B0784 E. coli 1563 Cytoplasmic 1701,1702 X_1 1 9 NUE_OE B0873 E. coli 1705 Plastidic 1831, 1832 X_1 1 10NUE_OE B1014 E. coli 1844 Cytoplasmic 1932, 1933 X_1 1 11 NUE_OE B1020E. coli 1950 Plastidic 1966, 1967 X_1 1 12 NUE_OE B1180 E. coli 1975Cytoplasmic 2121, 2122 X_1 1 13 NUE_OE B1933 E. coli 2127 Plastidic2133, 2134 X_1 1 14 NUE_OE B2032 E. coli 2135 Plastidic 2167, 2168 X_1 115 NUE_OE B2165 E. coli 2171 Plastidic 2289, 2290 X_1 1 16 NUE_OE B2223E. coli 2297 Plastidic 2419, 2420 X_1 1 17 NUE_OE B2238 E. coli 2426Plastidic 2444, 2445 X_1 1 17 NUE_OE B2238 E. coli 2426 Cytoplasmic2444, 2445 X_1 1 18 NUE_OE B2310 E. coli 2452 Plastidic 2544, 2545 X_1 119 NUE_OE B2431 E. coli 2551 Plastidic 2591, 2592 X_1 1 20 NUE_OE B2600E. coli 2600 Plastidic 2658, 2659 X_1 1 21 NUE_OE B2766 E. coli 2668Plastidic 2766, 2767 X_1 1 22 NUE_OE B2903 E. coli 2772 Cytoplasmic3100, 3101 X_1 1 23 NUE_OE B3117 E. coli 3117 Plastidic 3383, 3384 X_1 124 NUE_OE B3120 E. coli 3390 Plastidic 3394, 3395 X_1 1 25 NUE_OE B3216E. coli 3396 Plastidic 3466, 3467 X_1 1 26 NUE_OE B3451 E. coli 3470Plastidic 3556, 3557 X_1 1 27 NUE_OE B3791 E. coli 3563 Cytoplasmic3765, 3766 X_1 1 28 NUE_OE B3825 E. coli 3770 Plastidic 3864, 3865 X_1 129 NUE_OE YAL019W S. 3868 Cytoplasmic 3878, 3879 X_1 cerevisiae 1 30NUE_OE YAR035W S. 3895 Cytoplasmic 3941, 3942 X_1 cerevisiae 1 31 NUE_OEYBL021C S. 3953 Cytoplasmic 4107, 4108 X_1 cerevisiae 1 32 NUE_OEYBR055C S. 4111 Cytoplasmic 4141, 4142 X_1 cerevisiae 1 33 NUE_OEYBR128C S. 4149 Cytoplasmic 4157, 4158 X_1 cerevisiae 1 34 NUE_OEYBR159W S. 4162 Cytoplasmic 4228, 4229 X_1 cerevisiae 1 35 NUE_OEYBR243C S. 4235 Cytoplasmic 4271, 4272 X_1 cerevisiae 1 35 NUE_OEYBR243C S. 4235 Plastidic 4271, 4272 X_1 cerevisiae 1 36 NUE_OE YBR262CS. 4280 Cytoplasmic 4286, 4287 X_1 cerevisiae 1 37 NUE_OE YCR019W S.4288 Cytoplasmic 4306, 4307 X_1 cerevisiae 1 38 NUE_OE YDR070C S. 4315Cytoplasmic 4321, 4322 X_1 cerevisiae 1 39 NUE_OE YDR079W S. 4325Cytoplasmic 4331, 4332 X_1 cerevisiae 1 40 NUE_OE YDR123C S. 4335Cytoplasmic 4341, 4342 X_1 cerevisiae 1 41 NUE_OE YDR137W S. 4346Cytoplasmic 4352, 4353 X_1 cerevisiae 1 42 NUE_OE YDR294C S. 4361Cytoplasmic 4391, 4392 X_1 cerevisiae 1 42 NUE_OE YDR294C S. 4361Plastidic 4391, 4392 X_1 cerevisiae 1 43 NUE_OE YDR330W S. 4402Cytoplasmic 4424, 4425 X_1 cerevisiae 1 44 NUE_OE YDR355C S. 4431Cytoplasmic 4433, 4434 X_1 cerevisiae 1 45 NUE_OE YDR430C S. 4435Plastidic 4469, 4470 X_1 cerevisiae 1 46 NUE_OE YDR472W S. 4485Cytoplasmic 4497, 4498 X_1 cerevisiae 1 47 NUE_OE YDR497C S. 4506Plastidic 4786, 4787 X_1 cerevisiae 1 48 NUE_OE YER029C S. 4790Cytoplasmic 4800, 4801 X_1 cerevisiae 1 49 NUE_OE YFR007W S. 4806Cytoplasmic 4830, 4831 X_1 cerevisiae 1 50 NUE_OE YGL039W S. 4836Cytoplasmic 5306, 5307 X_1 cerevisiae 1 51 NUE_OE YGL043W S. 5311Cytoplasmic 5341, 5342 X_1 cerevisiae 1 52 NUE_OE YGR088W S. 5346Cytoplasmic 5526, 5527 X_1 cerevisiae 1 53 NUE_OE YGR122C-A S. 5533Cytoplasmic 5547, 5548 X_1 cerevisiae 1 54 NUE_OE YGR142W S. 5551Cytoplasmic 5557, 5558 X_1 cerevisiae 1 55 NUE_OE YGR143W S. 5559Cytoplasmic 5587, 5588 X_1 cerevisiae 1 56 NUE_OE YGR165W S. 5602Cytoplasmic 5606, 5607 X_1 cerevisiae 1 57 NUE_OE YGR170W S. 5608Cytoplasmic 5612, 5613 X_1 cerevisiae 1 58 NUE_OE YGR202C S. 5614Cytoplasmic 5660, 5661 X_1 cerevisiae 1 59 NUE_OE YGR266W S. 5666Cytoplasmic 5688, 5689 X_1 cerevisiae 1 60 NUE_OE YGR282C S. 5701Cytoplasmic 5741, 5742 X_1 cerevisiae 1 61 NUE_OE YGR290W S. 5750Cytoplasmic 5752, 5753 X_1 cerevisiae 1 62 NUE_OE YHL021C S. 5754Cytoplasmic 5770, 5771 X_1 cerevisiae 1 63 NUE_OE YHL031C S. 5778Cytoplasmic 5808, 5809 X_1 cerevisiae 1 64 NUE_OE YHR011W S. 5812Cytoplasmic 5960, 5961 X_1 cerevisiae 1 65 NUE_OE YHR127W S. 5967Cytoplasmic 5971, 5972 X_1 cerevisiae 1 66 NUE_OE YHR137W S. 5973Cytoplasmic 6021, 6022 X_1 cerevisiae 1 66 NUE_OE YHR137W S. 5973Plastidic 6021, 6022 X_1 cerevisiae 1 67 NUE_OE YIL099W S. 6027Cytoplasmic 6099, 6100 X_1 cerevisiae 1 67 NUE_OE YIL099W S. 6027Plastidic 6099, 6100 X_1 cerevisiae 1 68 NUE_OE YIL147C S. 6107Cytoplasmic 6133, 6134 X_1 cerevisiae 1 69 NUE_OE YIR034C S. 6150Cytoplasmic 6186, 6187 X_1 cerevisiae 1 70 NUE_OE YJL013C S. 6198Cytoplasmic 6206, 6207 X_1 cerevisiae 1 71 NUE_OE YJL041W S. 6208Cytoplasmic 6236, 6237 X_1 cerevisiae 1 72 NUE_OE YJL064W S. 6242Cytoplasmic 6244, 6245 X_1 cerevisiae 1 73 NUE_OE YJL067W S. 6246Cytoplasmic 6248, 6249 X_1 cerevisiae 1 74 NUE_OE YJL094C S. 6250Cytoplasmic 6286, 6287 X_1 cerevisiae 1 75 NUE_OE YJL171C S. 6297Cytoplasmic 6317, 6318 X_1 cerevisiae 1 76 NUE_OE YJL213W S. 6326Cytoplasmic 6482, 6483 X_1 cerevisiae 1 77 NUE_OE YJR017C S. 6488Cytoplasmic 6544, 6545 X_1 cerevisiae 1 78 NUE_OE YJR058C S. 6550Cytoplasmic 6696, 6697 X_1 cerevisiae 1 79 NUE_OE YJR117W S. 6700Cytoplasmic 6808, 6809 X_1 cerevisiae 1 80 NUE_OE YJR121W S. 6816Cytoplasmic 7350, 7351 X_1 cerevisiae 1 81 NUE_OE YJR131W S. 7366Cytoplasmic 7468, 7469 X_1 cerevisiae 1 82 NUE_OE YJR145C S. 7475Cytoplasmic 7597, 7598 X_1 cerevisiae 1 83 NUE_OE YKL084W S. 7602Cytoplasmic 7646, 7647 X_1 cerevisiae 1 84 NUE_OE YKL088W S. 7651Cytoplasmic 7655, 7656 X_1 cerevisiae 1 85 NUE_OE YKL100C S. 7661Cytoplasmic 7669, 7670 X_1 cerevisiae 1 86 NUE_OE YKL131W S. 7675Cytoplasmic 7677, 7678 X_1 cerevisiae 1 87 NUE_OE YKL138C S. 7679Cytoplasmic 7705, 7706 X_1 cerevisiae 1 88 NUE_OE YKL178C S. 7710Cytoplasmic 7720, 7721 X_1 cerevisiae 1 89 NUE_OE YKL179C S. 7735Cytoplasmic 7769, 7770 X_1 cerevisiae 1 90 NUE_OE YKL193C S. 7778Cytoplasmic 7822, 7823 X_1 cerevisiae 1 91 NUE_OE YKL216W S. 7829Cytoplasmic 8013, 8014 X_1 cerevisiae 1 92 NUE_OE YKR016W S. 8017Cytoplasmic 8039, 8040 X_1 cerevisiae 1 93 NUE_OE YKR021W S. 8045Cytoplasmic 8061, 8062 X_1 cerevisiae 1 94 NUE_OE YKR055W S. 8073Cytoplasmic 8259, 8260 X_1 cerevisiae 1 95 NUE_OE YKR088C S. 8263Plastidic 8281, 8282 X_1 cerevisiae 1 96 NUE_OE YKR093W S. 8287Cytoplasmic 8463, 8464 X_1 cerevisiae 1 97 NUE_OE YKR099W S. 8468Cytoplasmic 8474, 8475 X_1 cerevisiae 1 98 NUE_OE YKR100C S. 8484Cytoplasmic 8490, 8491 X_1 cerevisiae 1 99 NUE_OE YLL014W S. 8492Cytoplasmic 8510, 8511 X_1 cerevisiae 1 100 NUE_OE YLL016W S. 8514Cytoplasmic 8528, 8529 X_1 cerevisiae 1 101 NUE_OE YLL023C S. 8539Cytoplasmic 8567, 8568 X_1 cerevisiae 1 102 NUE_OE YLL037W S. 8571Cytoplasmic 8573, 8574 X_1 cerevisiae 1 103 NUE_OE YLL049W S. 8575Cytoplasmic 8577, 8578 X_1 cerevisiae 1 104 NUE_OE YLL055W S. 8579Cytoplasmic 8657, 8658 X_1 cerevisiae 1 105 NUE_OE YLR034C S. 8661Cytoplasmic 8983, 8984 X_1 cerevisiae 1 106 NUE_OE YLR042C S. 8991Cytoplasmic 8993, 8994 X_1 cerevisiae 1 107 NUE_OE YLR053C S. 8995Cytoplasmic 8997, 8998 X_1 cerevisiae 1 108 NUE_OE YLR058C S. 8999Cytoplasmic 9541, 9542 X_1 cerevisiae 1 109 NUE_OE YLR060W S. 9551Cytoplasmic 9629, 9630 X_1 cerevisiae 1 110 NUE_OE YLR065C S. 9637Cytoplasmic 9669, 9670 X_1 cerevisiae 1 111 NUE_OE YLR070C S. 9672Cytoplasmic 10178, 10179 X_1 cerevisiae 1 112 NUE_OE YLR100W S. 10182Cytoplasmic 10204, 10205 X_1 cerevisiae 1 113 NUE_OE YLR109W S. 10214Cytoplasmic 10444, 10445 X_1 cerevisiae 1 114 NUE_OE YLR125W S. 10447Cytoplasmic 10449, 10450 X_1 cerevisiae 1 115 NUE_OE YLR127C S. 10451Cytoplasmic 10461, 10462 X_1 cerevisiae 1 116 NUE_OE YLR185W S. 10463Cytoplasmic 10527, 10528 X_1 cerevisiae 1 117 NUE_OE YLR204W S. 10533Cytoplasmic 10539, 10540 X_1 cerevisiae 1 117 NUE_OE YLR204W S. 10533Plastidic 10539, 10540 X_1 cerevisiae 1 118 NUE_OE YLR242C S. 10541Cytoplasmic 10555, 10556 X_1 cerevisiae 1 119 NUE_OE YLR293C S. 10562Cytoplasmic 10984, 10985 X_1 cerevisiae 1 120 NUE_OE YLR313C S. 10990Cytoplasmic 10996, 10997 X_1 cerevisiae 1 121 NUE_OE YLR315W S. 10998Cytoplasmic 11002, 11003 X_1 cerevisiae 1 122 NUE_OE YLR329W S. 11004Cytoplasmic 11010, 11011 X_1 cerevisiae 1 123 NUE_OE YLR362W S. 11012Cytoplasmic 11044, 11045 X_1 cerevisiae 1 124 NUE_OE YLR395C S. 11054Cytoplasmic 11062, 11063 X_1 cerevisiae 1 125 NUE_OE YLR404W S. 11066Cytoplasmic 11072, 11073 X_1 cerevisiae 1 126 NUE_OE YLR463C S. 11074Cytoplasmic 11078, 11079 X_1 cerevisiae 1 127 NUE_OE YML022W S. 11080Cytoplasmic 11548, 11549 X_1 cerevisiae 1 128 NUE_OE YML027W S. 11552Cytoplasmic 11564, 11565 X_1 cerevisiae 1 129 NUE_OE YML065W S. 11569Cytoplasmic 11587, 11588 X_1 cerevisiae 1 130 NUE_OE YML089C S. 11596Cytoplasmic 11598, 11599 X_1 cerevisiae 1 131 NUE_OE YML128C S. 11600Cytoplasmic 11610, 11611 X_1 cerevisiae 1 132 NUE_OE YMR011W S. 11612Cytoplasmic 12242, 12243 X_1 cerevisiae 1 133 NUE_OE YMR037C S. 12246Cytoplasmic 12256, 12257 X_1 cerevisiae 1 134 NUE_OE YMR049C S. 12263Cytoplasmic 12299, 12300 X_1 cerevisiae 1 135 NUE_OE YMR052W S. 12316Cytoplasmic 12322, 12323 X_1 cerevisiae 1 136 NUE_OE YMR082C S. 12327Cytoplasmic 12329, 12330 X_1 cerevisiae 1 137 NUE_OE YMR125W S. 12331Cytoplasmic 12367, 12368 X_1 cerevisiae 1 138 NUE_OE YMR126C S. 12378Cytoplasmic 12386, 12387 X_1 cerevisiae 1 139 NUE_OE YMR144W S. 12394Cytoplasmic 12400, 12401 X_1 cerevisiae 1 140 NUE_OE YMR160W S. 12406Cytoplasmic 12412, 12413 X_1 cerevisiae 1 141 NUE_OE YMR191W S. 12414Cytoplasmic 12418, 12419 X_1 cerevisiae 1 142 NUE_OE YMR209C S. 12420Cytoplasmic 12430, 12431 X_1 cerevisiae 1 143 NUE_OE YMR233W S. 12440Cytoplasmic 12466, 12467 X_1 cerevisiae 1 144 NUE_OE YMR278W S. 12470Cytoplasmic 12740, 12741 X_1 cerevisiae 1 145 NUE_OE YMR280C S. 12749Cytoplasmic 12757, 12758 X_1 cerevisiae 1 146 NUE_OE YNL014W S. 12773Cytoplasmic 12811, 12812 X_1 cerevisiae 1 147 NUE_OE YNL320W S. 12829Cytoplasmic 12875, 12876 X_1 cerevisiae 1 148 NUE_OE YOL007C S. 12883Cytoplasmic 12887, 12888 X_1 cerevisiae 1 149 NUE_OE YOL164W S. 12889Cytoplasmic 13001, 13002 X_1 cerevisiae 1 150 NUE_OE YOR076C S. 13014Cytoplasmic 13016, 13017 X_1 cerevisiae 1 151 NUE_OE YOR083W S. 13018Cytoplasmic 13022, 13023 X_1 cerevisiae 1 152 NUE_OE YOR097C S. 13024Cytoplasmic 13028, 13029 X_1 cerevisiae 1 153 NUE_OE YOR128C S. 13030Cytoplasmic 13100, 13101 X_1 cerevisiae 1 154 NUE_OE YOR353C S. 14085Cytoplasmic 14091, 14092 X_1 cerevisiae 1 155 NUE_OE YPL141C S. 14093Cytoplasmic 14101, 14102 X_1 cerevisiae 1 156 NUE_OE YPR088C S. 14113Cytoplasmic 14235, 14236 X_1 cerevisiae 1 157 NUE_OE YPR108W S. 14246Cytoplasmic 14300, 14301 X_1 cerevisiae 1 158 NUE_OE YPR110C S. 14311Cytoplasmic 14383, 14384 X_1 cerevisiae 1 159 NUE_OE B3825_2 E. coli14914 Plastidic 15010, 15011 X_1 1 160 NUE_OE YIR034C_2 S. 15382Cytoplasmic 15420, 15421 X_1 cerevisiae 1 161 NUE_OE YJR131W_2 S. 15460Cytoplasmic 15564, 15565 X_1 cerevisiae 1 162 NUE_OE YKL100C_2 S. 15571Cytoplasmic 15581, 15582 X_1 cerevisiae 1 163 NUE_OE YKL193C_2 S. 15593Cytoplasmic 15639, 15640 X_1 cerevisiae 1 164 NUE_OE YLL016W_2 S. 15646Cytoplasmic 15662, 15663 X_1 cerevisiae 1 165 NUE_OE YLR034C_2 S. 15673Cytoplasmic 15997, 15998 X_1 cerevisiae 1 166 NUE_OE YLR060W_2 S. 16005Cytoplasmic 16085, 16086 X_1 cerevisiae 1 167 NUE_OE YMR082C_2 S. 16114Cytoplasmic 16118, 16119 X_1 cerevisiae 1 168 NUE_OE B1258 E. coli 14402Cytoplasmic 14492, 14493 X_1 1 169 NUE_OE YML101C S. 16093 Cytoplasmic16101, 16102 X_1 cerevisiae 1 170 NUE_OE YMR065W S. 16106 Cytoplasmic16112, 16113 X_1 cerevisiae 1 171 NUE_OE YMR163C S. 16120 Cytoplasmic16128, 16129 X_1 cerevisiae 1 172 NUE_OE YOL042W S. 16275 Cytoplasmic16289, 16290 X_1 cerevisiae 1 173 NUE_OE YOR226C S. 16305 Cytoplasmic16567, 16568 X_1 cerevisiae 1 174 NUE_OE YPL068C S. 16573 Cytoplasmic16579, 16580 X_1 cerevisiae 1 175 NUE_OE B0165 E. coli 14396 Plastidic14400, 14401 X_1 1 176 NUE_OE YOR203W S. 16299 Cytoplasmic 16303, 16304X_1 cerevisiae 1 177 NUE_OE YNL147W S. 16133 Cytoplasmic 16271, 16272X_1 cerevisiae 1 178 NUE_OE YBR083W S. 15056 Cytoplasmic 15062, 15063X_1 cerevisiae 1 179 NUE_OE YKL111C S. 15587 Cytoplasmic 15591, 15592X_1 cerevisiae 1 180 NUE_OE YPR067W S. 16582 Cytoplasmic 16624, 16625X_1 cerevisiae 1 181 NUE_OE B1985 E. coli 14839 Cytoplasmic 14867, 14868X_1 1 182 NUE_OE B3838 E. coli 15014 Cytoplasmic 15050, 15051 X_1 1 183NUE_OE YJL010C S. 15432 Cytoplasmic 15450, 15451 X_1 cerevisiae 1 184NUE_OE B1267 E. coli 14497 Cytoplasmic 14713, 14714 X_1 1 185 NUE_OEB1322 E. coli 14718 Cytoplasmic 14786, 14787 X_1 1 186 NUE_OE B1381 E.coli 14791 Cytoplasmic 14821, 14822 X_1 1 187 NUE_OE B2646 E. coli 14879Cytoplasmic 14909, 14910 X_1 1 188 NUE_OE YBR191W S. 15064 Cytoplasmic15250, 15251 X_1 cerevisiae 1 189 NUE_OE YDL135C S. 15257 Cytoplasmic15373, 15374 X_1 cerevisiae 1 190 NUE_OE YHL005C S. 15378 Cytoplasmic15380, 15381 X_1 cerevisiae 1 191 NUE_OE YKR100C_2 S. 16629 Cytoplasmic16639, 16640 X_1 cerevisiae 1 192 NUE_OE YMR191W_2 S. 16647 Cytoplasmic16653, 16654 X_1 cerevisiae

TABLE IV Consensus amino acid sequence ID numbers 5. 7. 1. 2. 3. 4. Lead6. SEQ IDs of Consensus/ Application Hit Project Locus Organism SEQ IDTarget Pattern Sequences 1 1 NUE_OE B0017 E. coli 39 Cytoplasmic — X_1 12 NUE_OE B0045 E. coli 43 Cytoplasmic 120, 121, 122 X_1 1 3 NUE_OE B0180E. coli 124 Plastidic 377, 378, 379 X_1 1 4 NUE_OE B0242 E. coli 381Plastidic 672, 673, 674, 675, 676, 677, 678 X_1 1 5 NUE_OE B0403 E. coli680 Plastidic 803, 804, 805, 806, 807, 808, 809, 810, 811 X_1 1 6 NUE_OEB0474 E. coli 813 Cytoplasmic 1052, 1053, 1054 X_1 1 7 NUE_OE B0754 E.coli 1056 Plastidic 1553, 1554, 1555, 1556, 1557, 1558, 1559, 1560, X_11561, 1562 1 8 NUE_OE B0784 E. coli 1564 Cytoplasmic 1703, 1704 X_1 1 9NUE_OE B0873 E. coli 1706 Plastidic 1833, 1834, 1835, 1836, 1837, 1838,1839, 1840, X_1 1841, 1842, 1843 1 10 NUE_OE B1014 E. coli 1845Cytoplasmic 1934, 1935, 1936, 1937, 1938, 1939, 1940, 1941, X_1 1942,1943, 1944, 1945, 1946, 1947, 1948, 1949 1 11 NUE_OE B1020 E. coli 1951Plastidic 1968, 1969, 1970, 1971, 1972, 1973, 1974 X_1 1 12 NUE_OE B1180E. coli 1976 Cytoplasmic 2123, 2124, 2125, 2126 X_1 1 13 NUE_OE B1933 E.coli 2128 Plastidic — X_1 1 14 NUE_OE B2032 E. coli 2136 Plastidic 2169,2170 X_1 1 15 NUE_OE B2165 E. coli 2172 Plastidic 2291, 2292, 2293,2294, 2295, 2296 X_1 1 16 NUE_OE B2223 E. coli 2298 Plastidic 2421,2422, 2423, 2424, 2425 X_1 1 17 NUE_OE B2238 E. coli 2427 Plastidic2446, 2447, 2448, 2449, 2450, 2451 X_1 1 17 NUE_OE B2238 E. coli 2427Cytoplasmic 2446, 2447, 2448, 2449, 2450, 2451 X_1 1 18 NUE_OE B2310 E.coli 2453 Plastidic 2546, 2547, 2548, 2549, 2550 X_1 1 19 NUE_OE B2431E. coli 2552 Plastidic 2593, 2594, 2595, 2596, 2597, 2598, 2599 X_1 1 20NUE_OE B2600 E. coli 2601 Plastidic 2660, 2661, 2662, 2663, 2664, 2665,2666, 2667 X_1 1 21 NUE_OE B2766 E. coli 2669 Plastidic 2768, 2769,2770, 2771 X_1 1 22 NUE_OE B2903 E. coli 2773 Cytoplasmic 3102, 3103,3104, 3105, 3106, 3107, 3108, 3109, X_1 3110, 3111, 3112, 3113, 3114,3115, 3116 1 23 NUE_OE B3117 E. coli 3118 Plastidic 3385, 3386, 3387,3388, 3389 X_1 1 24 NUE_OE B3120 E. coli 3391 Plastidic — X_1 1 25NUE_OE B3216 E. coli 3397 Plastidic 3468, 3469 X_1 1 26 NUE_OE B3451 E.coli 3471 Plastidic 3558, 3559, 3560, 3561, 3562 X_1 1 27 NUE_OE B3791E. coli 3564 Cytoplasmic 3767, 3768, 3769 X_1 1 28 NUE_OE B3825 E. coli3771 Plastidic 3866, 3867 X_1 1 29 NUE_OE YAL019W S. 3869 Cytoplasmic3880, 3881, 3882, 3883, 3884, 3885, 3886, 3887, X_1 cerevisiae 3888,3889, 3890, 3891, 3892, 3893, 3894 1 30 NUE_OE YAR035W S. 3896Cytoplasmic 3943, 3944, 3945, 3946, 3947, 3948, 3949, 3950, X_1cerevisiae 3951, 3952 1 31 NUE_OE YBL021C S. 3954 Cytoplasmic 4109, 4110X_1 cerevisiae 1 32 NUE_OE YBR055C S. 4112 Cytoplasmic 4143, 4144, 4145,4145, 4147, 4148 X_1 cerevisiae 1 33 NUE_OE YBR128C S. 4150 Cytoplasmic4159, 4160, 4161 X_1 cerevisiae 1 34 NUE_OE YBR159W S. 4163 Cytoplasmic4230, 4231, 4232, 4233, 4234 X_1 cerevisiae 1 35 NUE_OE YBR243C S. 4236Cytoplasmic 4273, 4274, 4275, 4276, 4277, 4278, 4279 X_1 cerevisiae 1 35NUE_OE YBR243C S. 4236 Plastidic 4273, 4274, 4275, 4276, 4277, 4278,4279 X_1 cerevisiae 1 36 NUE_OE YBR262C S. 4281 Cytoplasmic — X_1cerevisiae 1 37 NUE_OE YCR019W S. 4289 Cytoplasmic 4308, 4309, 4310,4311, 4312, 4313, 4314 X_1 cerevisiae 1 38 NUE_OE YDR070C S. 4316Cytoplasmic 4323, 4324 X_1 cerevisiae 1 39 NUE_OE YDR079W S. 4326Cytoplasmic 4333, 4334 X_1 cerevisiae 1 40 NUE_OE YDR123C S. 4336Cytoplasmic 4343, 4344, 4345 X_1 cerevisiae 1 41 NUE_OE YDR137W S. 4347Cytoplasmic 4354, 4355, 4356, 4357, 4358, 4359, 4360 X_1 cerevisiae 1 42NUE_OE YDR294C S. 4362 Cytoplasmic 4393, 4394, 4395, 4396, 4397, 4398,4399, 4400, X_1 cerevisiae 4401 1 42 NUE_OE YDR294C S. 4362 Plastidic4393, 4394, 4395, 4396, 4397, 4398, 4399, 4400, X_1 cerevisiae 4401 1 43NUE_OE YDR330W S. 4403 Cytoplasmic 4426, 4427, 4428, 4429, 4430 X_1cerevisiae 1 44 NUE_OE YDR355C S. 4432 Cytoplasmic — X_1 cerevisiae 1 45NUE_OE YDR430C S. 4436 Plastidic 4471, 4472, 4473, 4474, 4475, 4476,4477, 4478, X_1 cerevisiae 4479, 4480, 4481, 4482, 4483, 4484 1 46NUE_OE YDR472W S. 4486 Cytoplasmic 4499, 4500, 4501, 4502, 4503, 4504,4505 X_1 cerevisiae 1 47 NUE_OE YDR497C S. 4507 Plastidic 4788, 4789 X_1cerevisiae 1 48 NUE_OE YER029C S. 4791 Cytoplasmic 4802, 4803, 4804,4805 X_1 cerevisiae 1 49 NUE_OE YFR007W S. 4807 Cytoplasmic 4832, 4833,4834, 4835 X_1 cerevisiae 1 50 NUE_OE YGL039W S. 4837 Cytoplasmic 5308,5309, 5310 X_1 cerevisiae 1 51 NUE_OE YGL043W S. 5312 Cytoplasmic 5343,5344, 5345 X_1 cerevisiae 1 52 NUE_OE YGR088W S. 5347 Cytoplasmic 5528,5529, 5530, 5531, 5532 X_1 cerevisiae 1 53 NUE_OE YGR122C-A S. 5534Cytoplasmic 5549, 5550 X_1 cerevisiae 1 54 NUE_OE YGR142W S. 5552Cytoplasmic — X_1 cerevisiae 1 55 NUE_OE YGR143W S. 5560 Cytoplasmic5589, 5590, 5591, 5592, 5593, 5594, 5595, 5596, X_1 cerevisiae 5597,5598, 5599, 5600, 5601 1 56 NUE_OE YGR165W S. 5603 Cytoplasmic — X_1cerevisiae 1 57 NUE_OE YGR170W S. 5609 Cytoplasmic — X_1 cerevisiae 1 58NUE_OE YGR202C S. 5615 Cytoplasmic 5662, 5663, 5664, 5665 X_1 cerevisiae1 59 NUE_OE YGR266W S. 5667 Cytoplasmic 5690, 5691, 5692, 5693, 5694,5695, 5696, 5697, X_1 cerevisiae 5698, 5699, 5700 1 60 NUE_OE YGR282C S.5702 Cytoplasmic 5743, 5744, 5745, 5746, 5747, 5748, 5749 X_1 cerevisiae1 61 NUE_OE YGR290W S. 5751 Cytoplasmic — X_1 cerevisiae 1 62 NUE_OEYHL021C S. 5755 Cytoplasmic 5772, 5773, 5774, 5775, 5776, 5777 X_1cerevisiae 1 63 NUE_OE YHL031C S. 5779 Cytoplasmic 5810, 5811 X_1cerevisiae 1 64 NUE_OE YHR011W S. 5813 Cytoplasmic 5962, 5963, 5964,5965, 5966 X_1 cerevisiae 1 65 NUE_OE YHR127W S. 5968 Cytoplasmic — X_1cerevisiae 1 66 NUE_OE YHR137W S. 5974 Cytoplasmic 6023, 6024, 6025,6026 X_1 cerevisiae 1 66 NUE_OE YHR137W S. 5974 Plastidic 6023, 6024,6025, 6026 X_1 cerevisiae 1 67 NUE_OE YIL099W S. 6028 Cytoplasmictidic6101, 6102, 6103, 6104, 6105, 6106 X_1 cerevisiae 1 67 NUE_OE YIL099W S.6028 Plastidic 6101, 6102, 6103, 6104, 6105, 6106 X_1 cerevisiae 1 68NUE_OE YIL147C S. 6108 Cytoplasmic 6135, 6136, 6137, 6138, 6139, 6140,6141, 6142, X_1 cerevisiae 6143, 6144, 6145, 6146, 6147, 6148, 6149 1 69NUE_OE YIR034C S. 6151 Cytoplasmic 6188, 6189, 6190, 6191, 6192, 6193,6194, 6195, X_1 cerevisiae 6196, 6197 1 70 NUE_OE YJL013C S. 6199Cytoplasmic — X_1 cerevisiae 1 71 NUE_OE YJL041W S. 6209 Cytoplasmic6238, 6239, 6240, 6241 X_1 cerevisiae 1 72 NUE_OE YJL064W S. 6243Cytoplasmic — X_1 cerevisiae 1 73 NUE_OE YJL067W S. 6247 Cytoplasmic —X_1 cerevisiae 1 74 NUE_OE YJL094C S. 6251 Cytoplasmic 6288, 6289, 6290,6291, 6292, 6293, 6294, 6295, X_1 cerevisiae 6296 1 75 NUE_OE YJL171C S.6298 Cytoplasmic 6319, 6320, 6321, 6322, 6323, 6324, 6325 X_1 cerevisiae1 76 NUE_OE YJL213W S. 6327 Cytoplasmic 6484, 6485, 6486, 6487 X_1cerevisiae 1 77 NUE_OE YJR017C S. 6489 Cytoplasmic 6546, 6547, 6548,6549 X_1 cerevisiae 1 78 NUE_OE YJR058C S. 6551 Cytoplasmic 6698, 6699X_1 cerevisiae 1 79 NUE_OE YJR117W S. 6701 Cytoplasmic 6810, 6811, 6812,6813, 6814, 6815 X_1 cerevisiae 1 80 NUE_OE YJR121W S. 6817 Cytoplasmic7352, 7353, 7354, 7355, 7356, 7357, 7358, 7359, X_1 cerevisiae 7360,7361, 7362, 7363, 7364, 7365 1 81 NUE_OE YJR131W S. 7367 Cytoplasmic7470, 7471, 7472, 7473, 7474 X_1 cerevisiae 1 82 NUE_OE YJR145C S. 7476Cytoplasmic 7599, 7600, 7601 X_1 cerevisiae 1 83 NUE_OE YKL084W S. 7603Cytoplasmic 7648, 7649, 7650 X_1 cerevisiae 1 84 NUE_OE YKL088W S. 7652Cytoplasmic 7657, 7658, 7659, 7660 X_1 cerevisiae 1 85 NUE_OE YKL100C S.7662 Cytoplasmic 7671, 7672, 7673, 7674 X_1 cerevisiae 1 86 NUE_OEYKL131W S. 7676 Cytoplasmic — X_1 cerevisiae 1 87 NUE_OE YKL138C S. 7680Cytoplasmic 7707, 7708, 7709 X_1 cerevisiae 1 88 NUE_OE YKL178C S. 7711Cytoplasmic 7722, 7723, 7724, 7725, 7726, 7727, 7728, 7729, X_1cerevisiae 7730, 7731, 7732, 7733, 7734 1 89 NUE_OE YKL179C S. 7736Cytoplasmic 7771, 7772, 7773, 7774, 7775, 7776, 7777 X_1 cerevisiae 1 90NUE_OE YKL193C S. 7779 Cytoplasmic 7824, 7825, 7826, 7827, 7828 X_1cerevisiae 1 91 NUE_OE YKL216W S. 7830 Cytoplasmic 8015, 8016 X_1cerevisiae 1 92 NUE_OE YKR016W S. 8018 Cytoplasmic 8041, 8042, 8043,8044 X_1 cerevisiae 1 93 NUE_OE YKR021W S. 8046 Cytoplasmic 8063, 8064,8065, 8066, 8067, 8068, 8069, 8070, X_1 cerevisiae 8071, 8072 1 94NUE_OE YKR055W S. 8074 Cytoplasmic 8261, 8262 X_1 cerevisiae 1 95 NUE_OEYKR088C S. 8264 Plastidic 8283, 8284, 8285, 8286 X_1 cerevisiae 1 96NUE_OE YKR093W S. 8288 Cytoplasmic 8465, 8466, 8467 X_1 cerevisiae 1 97NUE_OE YKR099W S. 8469 Cytoplasmic 8476, 8477, 8478, 8479, 8480, 8481,8482, 8483 X_1 cerevisiae 1 98 NUE_OE YKR100C S. 8485 Cytoplasmic — X_1cerevisiae 1 99 NUE_OE YLL014W S. 8493 Cytoplasmic 8512, 8513 X_1cerevisiae 1 100 NUE_OE YLL016W S. 8515 Cytoplasmic 8530, 8531, 8532,8533, 8534, 8535, 8536, 8537, X_1 cerevisiae 8538 1 101 NUE_OE YLL023CS. 8540 Cytoplasmic 8569, 8570 X_1 cerevisiae 1 102 NUE_OE YLL037W S.8572 Cytoplasmic — X_1 cerevisiae 1 103 NUE_OE YLL049W S. 8576Cytoplasmic — X_1 cerevisiae 1 104 NUE_OE YLL055W S. 8580 Cytoplasmic8659, 8660 X_1 cerevisiae 1 105 NUE_OE YLR034C S. 8662 Cytoplasmic 8985,8986, 8987, 8988, 8989, 8990 X_1 cerevisiae 1 106 NUE_OE YLR042C S. 8992Cytoplasmic — X_1 cerevisiae 1 107 NUE_OE YLR053C S. 8996 Cytoplasmic —X_1 cerevisiae 1 108 NUE_OE YLR058C S. 9000 Cytoplasmic 9543, 9544,9545, 9546, 9547, 9548, 9549, 9550 X_1 cerevisiae 1 109 NUE_OE YLR060WS. 9552 Cytoplasmic 9631, 9632, 9633, 9634, 9635, 9636 X_1 cerevisiae 1110 NUE_OE YLR065C S. 9638 Cytoplasmic 9671 X_1 cerevisiae 1 111 NUE_OEYLR070C S. 9673 Cytoplasmic 10180, 10181 X_1 cerevisiae 1 112 NUE_OEYLR100W S. 10183 Cytoplasmic 10206, 10207, 10208, 10209, 10210, 10211,10212, X_1 cerevisiae 10213 1 113 NUE_OE YLR109W S. 10215 Cytoplasmic10446 X_1 cerevisiae 1 114 NUE_OE YLR125W S. 10448 Cytoplasmic — X_1cerevisiae 1 115 NUE_OE YLR127C S. 10452 Cytoplasmic — X_1 cerevisiae 1116 NUE_OE YLR185W S. 10464 Cytoplasmic 10529, 10530, 10531, 10532 X_1cerevisiae 1 117 NUE_OE YLR204W S. 10534 Cytoplasmic — X_1 cerevisiae 1117 NUE_OE YLR204W S. 10534 Plastidic — X_1 cerevisiae 1 118 NUE_OEYLR242C S. 10542 Cytoplasmic 10557, 10558, 10559, 10560, 10561 X_1cerevisiae 1 119 NUE_OE YLR293C S. 10563 Cytoplasmic 10986, 10987,10988, 10989 X_1 cerevisiae 1 120 NUE_OE YLR313C S. 10991 Cytoplasmic —X_1 cerevisiae 1 121 NUE_OE YLR315W S. 10999 Cytoplasmic — X_1cerevisiae 1 122 NUE_OE YLR329W S. 11005 Cytoplasmic — X_1 cerevisiae 1123 NUE_OE YLR362W S. 11013 Cytoplasmic 11046, 11047, 11048, 11049,11050, 11051, 11052, X_1 cerevisiae 11053 1 124 NUE_OE YLR395C S. 11055Cytoplasmic 11064, 11065 X_1 cerevisiae 1 125 NUE_OE YLR404W S. 11067Cytoplasmic — X_1 cerevisiae 1 126 NUE_OE YLR463C S. 11075 Cytoplasmic —X_1 cerevisiae 1 127 NUE_OE YML022W S. 11081 Cytoplasmic 11550, 11551X_1 cerevisiae 1 128 NUE_OE YML027W S. 11553 Cytoplasmic 11566, 11567,11568 X_1 cerevisiae 1 129 NUE_OE YML065W S. 11570 Cytoplasmic 11589,11590, 11591, 11592, 11593, 11594, 11595 X_1 cerevisiae 1 130 NUE_OEYML089C S. 11597 Cytoplasmic — X_1 cerevisiae 1 131 NUE_OE YML128C S.11601 Cytoplasmic — X_1 cerevisiae 1 132 NUE_OE YMR011W S. 11613Cytoplasmic 12244, 12245 X_1 cerevisiae 1 133 NUE_OE YMR037C S. 12247Cytoplasmic 12258, 12259, 12260, 12261, 12262 X_1 cerevisiae 1 134NUE_OE YMR049C S. 12264 Cytoplasmic 12301, 12302, 12303, 12304, 12305,12306, 12307, X_1 cerevisiae 12308, 12309, 12310, 12311, 12312, 12313,12314, 12315 1 135 NUE_OE YMR052W S. 12317 Cytoplasmic 12324, 12325,12326 X_1 cerevisiae 1 136 NUE_OE YMR082C S. 12328 Cytoplasmic — X_1cerevisiae 1 137 NUE_OE YMR125W S. 12332 Cytoplasmic 12369, 12370,12371, 12372, 12373, 12374, 12375, X_1 cerevisiae 12376, 12377 1 138NUE_OE YMR126C S. 12379 Cytoplasmic 12388, 12389, 12390, 12391, 12392,12393 X_1 cerevisiae 1 139 NUE_OE YMR144W S. 12395 Cytoplasmic 12402,12403, 12404, 12405 X_1 cerevisiae 1 140 NUE_OE YMR160W S. 12407Cytoplasmic — X_1 cerevisiae 1 141 NUE_OE YMR191W S. 12415 Cytoplasmic —X_1 cerevisiae 1 142 NUE_OE YMR209C S. 12421 Cytoplasmic 12432, 12433,12434, 12435, 12436, 12437, 12438, X_1 cerevisiae 12439 1 143 NUE_OEYMR233W S. 12441 Cytoplasmic 12468, 12469 X_1 cerevisiae 1 144 NUE_OEYMR278W S. 12471 Cytoplasmic 12742, 12743, 12744, 12745, 12746, 12747,12748 X_1 cerevisiae 1 145 NUE_OE YMR280C S. 12750 Cytoplasmic 12759,12760, 12761, 12762, 12763, 12764, 12765, X_1 cerevisiae 12766, 12767,12768, 12769, 12770, 12771, 12772 1 146 NUE_OE YNL014W S. 12774Cytoplasmic 12813, 12814, 12815, 12816, 12817, 12818, 12819, X_1cerevisiae 12820, 12821, 12822, 12823, 12824, 12825, 12826, 12827, 128281 147 NUE_OE YNL320W S. 12830 Cytoplasmic 12877, 12878, 12879, 12880,12881, 12882 X_1 cerevisiae 1 148 NUE_OE YOL007C S. 12884 Cytoplasmic —X_1 cerevisiae 1 149 NUE_OE YOL164W S. 12890 Cytoplasmic 13003, 13004,13005, 13006, 13007, 13008, 13009, X_1 cerevisiae 13010, 13011, 13012,13013 1 150 NUE_OE YOR076C S. 13015 Cytoplasmic — X_1 cerevisiae 1 151NUE_OE YOR083W S. 13019 Cytoplasmic — X_1 cerevisiae 1 152 NUE_OEYOR097C S. 13025 Cytoplasmic — X_1 cerevisiae 1 153 NUE_OE YOR128C S.13031 Cytoplasmic 13102, 13103, 13104, 13105, 13106, 13107, 13108, X_1cerevisiae 13109, 13110, 13111, 13112, 13113, 13114 1 154 NUE_OE YOR353CS. 14086 Cytoplasmic — X_1 cerevisiae 1 155 NUE_OE YPL141C S. 14094Cytoplasmic 14103, 14104, 14105, 14106, 14107, 14108, 14109, X_1cerevisiae 14110, 14111, 14112 1 156 NUE_OE YPR088C S. 14114 Cytoplasmic14237, 14238, 14239, 14240, 14241, 14242, 14243, X_1 cerevisiae 14244,14245 1 157 NUE_OE YPR108W S. 14247 Cytoplasmic 14302, 14303, 14304,14305, 14306, 14307, 14308, X_1 cerevisiae 14309, 14310 1 158 NUE_OEYPR110C S. 14312 Cytoplasmic 14385, 14386, 14387, 14388 X_1 cerevisiae 1159 NUE_OE B3825_2 E. coli 14915 Plastidic 15012, 15013 X_1 1 160 NUE_OEYIR034C_2 S. 15383 Cytoplasmic 15422, 15423, 15424, 15425, 15426, 15427,15428, X_1 cerevisiae 15429, 15430, 15431 1 161 NUE_OE YJR131W_2 S.15461 Cytoplasmic 15566, 15567, 15568, 15569, 15570 X_1 cerevisiae 1 162NUE_OE YKL100C_2 S. 15572 Cytoplasmic 15583, 15584, 15585, 15586 X_1cerevisiae 1 163 NUE_OE YKL193C_2 S. 15594 Cytoplasmic 15641, 15642,15643, 15644, 15645 X_1 cerevisiae 1 164 NUE_OE YLL016W_2 S. 15647Cytoplasmic 15664, 15665, 15666, 15667, 15668, 15669, 15670, X_1cerevisiae 15671, 15672 1 165 NUE_OE YLR034C_2 S. 15674 Cytoplasmic15999, 16000, 16001, 16002, 16003, 16004 X_1 cerevisiae 1 166 NUE_OEYLR060W_2 S. 16006 Cytoplasmic 16087, 16088, 16089, 16090, 16091, 16092X_1 cerevisiae 1 167 NUE_OE YMR082C_2 S. 16115 Cytoplasmic — X_1cerevisiae 1 168 NUE_OE B1258 E. coli 14403 Cytoplasmic 14494, 14495,14496 X_1 1 169 NUE_OE YML101C S. 16094 Cytoplasmic 16103, 16104, 16105X_1 cerevisiae 1 170 NUE_OE YMR065W S. 16107 Cytoplasmic — X_1cerevisiae 1 171 NUE_OE YMR163C S. 16121 Cytoplasmic 16130, 16131, 16132X_1 cerevisiae 1 172 NUE_OE YOL042W S. 16276 Cytoplasmic 16291, 16292,16293, 16294, 16295, 16296, 16297, X_1 cerevisiae 16298 1 173 NUE_OEYOR226C S. 16306 Cytoplasmic 16569, 16570, 16571, 16572 X_1 cerevisiae 1174 NUE_OE YPL068C S. 16574 Cytoplasmic 16581 X_1 cerevisiae 1 175NUE_OE B0165 E. coli 14397 Plastidic — X_1 1 176 NUE_OE YOR203W S. 16300Cytoplasmic — X_1 cerevisiae 1 177 NUE_OE YNL147W S. 16134 Cytoplasmic16273, 16274 X_1 cerevisiae 1 178 NUE_OE YBR083W S. 15057 Cytoplasmic —X_1 cerevisiae 1 179 NUE_OE YKL111C S. 15588 Cytoplasmic — X_1cerevisiae 1 180 NUE_OE YPR067W S. 16583 Cytoplasmic 16626, 16627, 16628X_1 cerevisiae 1 181 NUE_OE B1985 E. coli 14840 Cytoplasmic 14869,14870, 14871, 14872, 14873, 14874, 14875, X_1 14876, 14877, 14878 1 182NUE_OE B3838 E. coli 15015 Cytoplasmic 15052, 15053, 15054, 15055 X_1 1183 NUE_OE YJL010C S. 15433 Cytoplasmic 15452, 15453, 15454, 15455,15456, 15457, 15458, X_1 cerevisiae 15459 1 184 NUE_OE B1267 E. coli14498 Cytoplasmic 14715, 14716, 14717 X_1 1 185 NUE_OE B1322 E. coli14719 Cytoplasmic 14788, 14789, 14790 X_1 1 186 NUE_OE B1381 E. coli14792 Cytoplasmic 14823, 14824, 14825, 14826, 14827, 14828, 14829, X_114830, 14831, 14832, 14833, 14834, 14835, 14836, 14837, 14838 1 187NUE_OE B2646 E. coli 14880 Cytoplasmic 14911, 14912, 14913 X_1 1 188NUE_OE YBR191W S. 15065 Cytoplasmic 15252, 15253, 15254, 15255, 15256X_1 cerevisiae 1 189 NUE_OE YDL135C S. 15258 Cytoplasmic 15375, 15376,15377 X_1 cerevisiae 1 190 NUE_OE YHL005C S. 15379 Cytoplasmic — X_1cerevisiae 1 191 NUE_OE YKR100C_2 S. 16630 Cytoplasmic 16641, 16642,16643, 16644, 16645, 16646 X_1 cerevisiae 1 192 NUE_OE YMR191W_2 S.16648 Cytoplasmic — X_1 cerevisiae

1. A method for producing a transgenic plant, plant cell or plant partwith increased yield, enhanced nitrogen use efficiency (NUE) and/orincreased biomass production as compared to a correspondingnon-transformed wild type plant, plant cell or plant part, comprisingincreasing or generating in a plant, plant cell or plant part one ormore activities selected from the group consisting of 3-keto sterolreductase, 60S ribosomal protein, adenine phosphoribosyltransferase,adenylate kinase, alkyl hydroperoxide reductase, Alkyl/aryl-sulfatase,alpha-glucosidase, alpha-mannosidase, anaphase promoting complex (APC)subunit, antiviral adaptor protein, aromatic amino acid aminotransferaseII, ARV1 protein, autophagy-specific phosphatidylinositol 3-kinasecomplex protein subunit, b0017-protein, B0165-protein, B1258-protein,B1267-protein, B1381-protein, b1933-protein, b2165-protein,b2238-protein, b2431-protein, B2646-protein, b2766-protein,b3120-protein, carnitine acetyltransferase, cell wallendo-beta-1,3-glucanase, chaperone, Chitin synthase 3 complex protein,cholinephosphate cytidylyltransferase, chorismate mutase T/prephenatedehydrogenase (bifunctional), clathrin associated protein complex smallsubunit, component of the RAM signaling network, cysteine transporter,cytochrome c oxidase subunit VIII, cytosolic catalase, cytosolic serinehydroxymethyltransferase, dihydroorotate dehydrogenase,dihydrosphingosine phosphate lyase, exoribonuclease, F1F0 ATP synthasebeta subunit, Factor arrest protein, G protein coupled pheromonereceptor receptor, gamma-glutamyl kinase, glucoamylase,glycerol-3-phosphate transporter subunit, glycine decarboxylase,glycosyltransferase, golgi membrane exchange factor subunit, golgimembrane protein, GPI-anchored cell wall protein, GTP-binding protein,helix-loop-helix transcription activator that bindsinositol/choline-responsive elements, hexose transporter, histidinekinase osmosensor that regulates an osmosensing MAP kinase cascade,hydro-lyase, hydroxylamine reductase, hydroxymyristol acyl carrierprotein dehydratase, inheritance of peroxisomes protein, integralmembrane protein localized to late Golgi vesicles, iron sulfur clusterassembly protein, isomerase, lysine/arginine/ornithine transportersubunit, lysine-specific metalloprotease, lysophospholipase, Mcm1pbinding transcriptional repressor, Meiotic recombination protein,membrane protein, metal ion transporter, microsomal beta-keto-reductase,mitochondrial intermembrane space protein, mitochondrial protein,mitochondrial ribosomal protein of the large subunit, mitochondrialribosomal protein of the small subunit, mitochondrial seryl-tRNAsynthetase, molybdopterin biosynthesis protein, myo-inositoltransporter, non-essential kinetochore protein, non-essential Rasguanine nucleotide exchange factor, non-essential small GTPase of theRho/Rac subfamily of Ras-like proteins, Nuclear cap-binding proteincomplex subunit, nuclear fusion protein precursor, nuclear pore complexsubunit, origin recognition complex subunit, outer membrane usherprotein, oxidoreductase, peptide transporter, peptidyl-prolyl cis-transisomerase, PhoH-like protein, phosphatidylserine decarboxylase,phosphoglucomutase/phosphomannomutase, phosphopantothenoylcysteinedecarboxylase, Phosphoribosylaminoimidazole carboxylase,potassium:hydrogen antiporter, proline dehydrogenase, protein componentof the large ribosomal subunit, protein involved in shmoo formation andbipolar bud site selection, protein involved in sphingolipidbiosynthesis, protein kinase, protein necessary for structural stabilityof L-A double-stranded RNA-containing particles, protein required formaturation of ribosomal RNAs, protein translocase protein, RegulatoryCAT8 protein, regulatory subunit of Glc7p type 1 proteinserine-threonine phosphatase, regulatory subunit of the 26S proteasome,repressor of G1 transcription, Rho GDP-dissociation inhibitor,ribonucleoprotein, ribosomal protein of the small subunit, RNApolymerase III subunit, saccharopine dehydrogenase, short chain fattyacid transporter, signal recognition particle subunit (SRP54), signaltransducing MEK kinase, SM complex B protein for mRNA splicing, spindlecheckpoint complex subunit, splicing factor, Stationary phase protein,subunit of cytoplasmic phenylalanyl-tRNA synthetase, subunit of thetransport protein particle (TRAPP) complex of the cis-Golgi, threonineammonia-lyase, transcription elongation factor, transcription factor,Transcriptional activator, translational elongation factor EF-3 (HEF3),transmembrane protein with a role in cell wall polymer composition,transport protein, ubiquitin regulatory protein,UDP-N-acetyl-glucosamine-1-P transferase, v-SNARE binding protein,v-SNARE protein involved in Golgi transport, xylitol dehydrogenase,yal019w-protein, ybr262c-protein, YDR070C-protein, ydr355c-protein,YFR007W-protein, ygr122c-a-protein, ygr266w-protein, ygr290w-protein,YHL005C-protein, yhl021c-protein, yhr127w-protein, YJL010C-protein,yjl064w-protein, yjl067w-protein, yjl213w-protein, ykl100c-protein,YKL111C-protein, ykl131w-protein, ykr016w-protein, ykr021w-protein,yll014w-protein, yll023c-protein, yll037w-protein, yll049w-protein,ylr042c-protein, YLR053c-protein, ylr065c-protein, ylr125w-protein,ylr404w-protein, ylr463c-protein, yml089c-protein, YML101C-protein,yml128c-protein, YMR082C-protein, YMR126c membrane protein,YMR144W-protein, YMR160W-protein, YMR209C-protein, YMR233W-protein,YNL320W-protein, YOR097c-protein, YOR203W-protein, YPL068C-protein, Zincfinger protein, and zinc metalloprotease.
 2. A method for producing atransgenic plant, plant cell or plant part with increased yield,enhanced nitrogen use efficiency (NUE) and/or increased biomassproduction as compared to a corresponding non-transformed wild typeplant, plant cell or plant part, comprising increasing or generating ina plant, plant cell or plant part the expression and/or activity of apolypeptide encoded by a nucleic acid molecule selected from the groupconsisting of: (a) a nucleic acid molecule encoding the polypeptideshown in column 5 or 7 of table II; (b) a nucleic acid molecule shown incolumn 5 or 7 of table I; (c) a nucleic acid molecule having at least30% sequence identity to any one of the nucleic acid molecules shown incolumn 5 or 7 of table I and conferring increased yield, enhanced NUEand/or increased biomass production when expressed in a plant, plantcell or plant part as compared to a corresponding non-transformed wildtype plant, plant cell or plant part; (d) a nucleic acid moleculeencoding a polypeptide having at least 30% sequence identity to any oneof the polypeptides shown in column 5 or 7 of table II and conferringincreased yield, enhanced NUE and/or increased biomass production whenexpressed in a plant, plant cell or plant part as compared to acorresponding non-transformed wild type plant, plant cell or plant part;(e) a nucleic acid molecule which hybridizes with the nucleic acidmolecule of (a) or (b) under stringent hybridization conditions andconfers increased yield, enhanced NUE and/or increased biomassproduction when expressed in a plant, plant cell or plant part ascompared to a corresponding non-transformed wild type plant, plant cellor plant part; and (f) a nucleic acid molecule encoding a polypeptidecomprising one or more polypeptide motifs as shown in column 7 of tableIV and conferring increased yield, enhanced NUE and/or increased biomassproduction when expressed in a plant, plant cell or plant part ascompared to a corresponding non-transformed wild type plant, plant cellor plant part, and optionally selecting for a plant, plant cell or plantpart with increased yield, enhanced nitrogen use efficiency (NUE) and/orincreased biomass production as compared to a correspondingnon-transformed wild type plant, plant cell or plant part.
 3. The methodof claim 2, wherein the expression and/or activity of said polypeptideis increased or generated by transforming said nucleic acid moleculeinto said plant, plant cell or plant part.
 4. The method of claim 2,wherein said transgenic plant, plant cell or plant part has increasedyield, enhanced nitrogen use efficiency (NUE) and/or increased biomassproduction as compared to a corresponding non-transformed wild typeplant, plant cell or plant part under standard growth conditions.
 5. Atransgenic plant, plant cell or plant part obtained by the method ofclaim 2, wherein said transgenic plant, plant cell or plant part hasincreased yield, enhanced nitrogen use efficiency (NUE) and/or increasedbiomass production as compared to a corresponding non-transformed wildtype plant, plant cell or plant part.
 6. The transgenic plant, plantcell or plant part of claim 5, wherein said plant is, or said plant cellor plant part is from, a monocotyledonous plant or a dicotyledonousplant.
 7. The transgenic plant, plant cell or plant part of claim 5,wherein said plant is, or said plant cell or plant part is from, a plantselected from the group consisting of maize, wheat, rye, oat, triticale,rice, barley, soybean, peanut, cotton, oil seed rape, canola, winter oilseed rape, cotton, corn, manihot, pepper, sunflower, flax, borage,safflower, linseed, primrose, rapeseed, turnip rape, tagetes,solanaceous plants, potato, tobacco, eggplant, tomato, Vicia species,pea, alfalfa, coffee, cacao, tea, Salix species, oil palm, coconut,perennial grass, forage crops and Arabidopsis thaliana.
 8. Seeds orprogeny of the transgenic plant of claim 5, wherein said seeds orprogeny comprise a recombinant nucleic acid molecule encoding saidpolypeptide.
 9. Harvestable parts of the transgenic plant of claim 5,wherein said harvestable parts comprise a recombinant nucleic acidmolecule encoding said polypeptide.
 10. An isolated recombinant nucleicacid molecule selected from the group consisting of: (a) a nucleic acidmolecule encoding the polypeptide shown in column 5 or 7 of table II B;(b) a nucleic acid molecule shown in column 5 or 7 of table I B; (c) anucleic acid molecule having at least 30% sequence identity to any oneof the nucleic acid molecules shown in column 5 or 7 of table I andconferring increased yield, enhanced NUE and/or increased biomassproduction when expressed in a plant, plant cell or plant part ascompared to a corresponding non-transformed wild type plant, plant cellor plant part; (d) a nucleic acid molecule encoding a polypeptide havingat least 30% sequence identity to any one of the polypeptides shown incolumn 5 or 7 of table II and conferring increased yield, enhanced NUEand/or increased biomass production when expressed in a plant, plantcell or plant part as compared to a corresponding non-transformed wildtype plant, plant cell or plant part; (e) a nucleic acid molecule whichhybridizes with the nucleic acid molecule of (a) or (b) under stringenthybridization conditions and confers increased yield, enhanced NUEand/or increased biomass production when expressed in a plant, plantcell or plant part as compared to a corresponding non-transformed wildtype plant, plant cell or plant part; and (f) a nucleic acid moleculeencoding a polypeptide comprising one or more polypeptide motifs asshown in column 7 of table IV and conferring increased yield, enhancedNUE and/or increased biomass production when expressed in a plant, plantcell or plant part as compared to a corresponding non-transformed wildtype plant, plant cell or plant part.
 11. An expression constructcomprising the isolated recombinant nucleic acid molecule of claim 10.12. A vector comprising: (a) the isolated recombinant nucleic acidmolecule of claim 10; or (b) an expression construct comprising theisolated recombinant nucleic acid molecule of (a).
 13. A non-human hostcell comprising: (a) the isolated recombinant nucleic acid molecule ofclaim 10; (b) an expression construct comprising the isolatedrecombinant nucleic acid molecule of (a); or (c) a vector comprising theisolated recombinant nucleic acid molecule of (a) or the expressionconstruct of (b).
 14. A process for producing a polypeptide comprisingproducing a polypeptide in the non-human host cell of claim
 13. 15. Atransgenic plant, plant cell or plant part comprising: (a) the isolatedrecombinant nucleic acid molecule of claim 10; (b) an expressionconstruct comprising the isolated recombinant nucleic acid molecule of(a); or (c) a vector comprising the isolated recombinant nucleic acidmolecule of (a) or the expression construct of (b).
 16. The transgenicplant, plant cell or plant part of claim 15, wherein said transgenicplant, plant cell or plant part shows improved nutrient use efficiency,improved abiotic stress tolerance, or both improved nutrient useefficiency and improved abiotic stress tolerance.
 17. The transgenicplant, plant cell or plant part of claim 15, wherein said transgenicplant, plant cell or plant part shows enhanced NUE.
 18. The transgenicplant, plant cell or plant part of claim 15, wherein said transgenicplant, plant cell or plant part shows increased low temperaturetolerance and/or increased tolerance to drought conditions.
 19. Thetransgenic plant, plant cell or plant part of claim 15, wherein saidtransgenic plant, plant cell or plant part has increased yield in theabsence of stress as well as nutrient deficiency.
 20. A method forproducing a transgenic plant, plant cell or plant part with increasedyield, enhanced nitrogen use efficiency (NUE) and/or increased biomassproduction as compared to a corresponding non-transformed wild typeplant, plant cell or plant part, comprising: (a) transforming a plant,plant cell or plant part an expression vector comprising the isolatedrecombinant nucleic acid molecule of claim 10; (b) generating from theplant cell or plant part a transgenic plant; and (c) selecting for atransgenic plant having increased yield, enhanced nitrogen useefficiency (NUE) and/or increased biomass production as compared to acorresponding non-transformed wild type plant.